Advances in the role of a plant coagulant ( Cynara cardunculus ) in vitro and during ripening of cheeses from several milk species

May combine two claims.

A few problems were encountered in experiments on French and Italian cheeses; these included slightly more acid and bitter flavours and softer curd, with concomitant increased tendencies for loss of shape.

“However, a few problems were encountered; these included slightly more acid and bitter flavours and softer curd, with concomitant increased tendencies for loss of shape [2,3].”

• cites [2] 2. Barbosa M., Valles E., Vassal L., Mocquot G., L'utilisation d'extrait de Cynara cardunculus L. comme agent coagulant en fabrication de fromages à pâte molle et à pâte cuite, Lait 56 (1976) 1-17. sourcePartly supported

  The organoleptic findings (section 5, page unavailable) report that Cynara-made cheeses were softer and became deformed during ripening. The paper also reports bitterness in Camembert and Gruyère, describing it as pronounced rather than slight. These passages do not report a more acidic flavour or experiments on Italian cheeses. (LLM, conf=0.89)

  Experimental — accuracy not yet measured
• cites [3] 3. Barbosa M., Corradini C., Battistoni B., Cheesemaking experiments carried out on some Italian cheeses with vegetable rennet from cardo (Cynara cardunculus L.), Sci. Tec. Latt.- Casearia 32 (1981) 203-221.Not checked — no full text of the source

Probably not a substantial claim: may not pass S3 (load-bearing).

NaCl has no significant effect on the rate of enzyme extraction.

“Salt may be added to the initial aqueous infusion, although it has been shown that NaCl has no significant effect on the rate of enzyme extraction [50,62].”

• cites [50] 50. Sousa M.J., Malcata F.X., Effects of processing conditions on the caseinolytic activity of pro- teinases from Cynara cardunculus L., Food Sci. Technol. Int. 2 (1996) 255-263.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

• cites [62] 62. Tsouli J., Étude comparée de l'activité enzymatique de trois varietés d'artichauts du genre Cynara cardunculus L. sur la coagulation du lait, Lait 44 (1974) 415-421. sourceSupported

Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.

Those two enzymes appear chiefly in the female part of the flowers of C. cardunculus, i.e. in the upper portion (where the ratio of concentrations of cardosin A to cardosin B is also higher); in the lower portion, only cardosin B is present.

“More recent studies [21,63,64] have indicated that those two enzymes appear chiefly in the female part of the flowers of C. cardunculus, i.e. in the upper portion (where the ratio of concentrations of cardosin A to cardosin B is also higher); in the lower portion, only cardosin B is present [9].”

• cites [21] 21. Faro C.J., Veríssimo P., Lin Y., Tang J., Pires E.V., in: Takahashi K. (Ed.), Aspartic protein- ases: Structure, Function, Biology and Biomed- ical Implications, Plenum Press, New York, USA, 1995, pp. 373-377.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

• cites [63] 63. Veríssimo P., Esteves C., Faro C., Pires E., The vegetable rennet of Cynara cardunculus L. con- tains two proteinases with chymosin and pepsin- like specificities, Biotechnol. Lett. 17 (1995) 621-626.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

• cites [64] 64. Veríssimo P., Faro C., Moir A.J., Lin Y., Tang J., Pires E., Purification, characterization and par- tial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L., Eur. J. Biochem. 235 (1996) 762-768. sourcePartly supported

  Split into 2 atoms — 0 confirmed, 1 partially supported, 0 disputed, 0 misattributed, 1 unverifiable. Expand the claim to see per-atom verdicts.

  Experimental — accuracy not yet measured
• cites [9] 9. Castanheira P.M.D., Distribuição diferencial das cardosinas A e B ao longo do pistilo de Cynara cardunculus L., MSc thesis, Universidade de Coimbra, Coimbra, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

These proteinases share pH optima in the acid range, inhibition by pepstatin and preferential cleavage of peptide bonds between hydrophobic residues.

“These proteinases share pH optima in the acid range, inhibition by pepstatin and preferential cleavage of peptide bonds between hydrophobic residues (as happens with other aspartic proteinases) [64].”

• cites [64] 64. Veríssimo P., Faro C., Moir A.J., Lin Y., Tang J., Pires E., Purification, characterization and par- tial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L., Eur. J. Biochem. 235 (1996) 762-768. sourceSupported

May combine two claims.

The bond Tyr95-Leu96 is also cleaved in bovine αs2-casein, whereas the bonds Ser9-Ser10 and Tyr179-Leu180 are cleaved in caprine caseinate as well.

“The bond Tyr 95 -Leu 96 was also cleaved in bovine α s2 -casein [32], whereas the bonds Ser 9 -Ser 10 and Tyr 179 -Leu 180 were cleaved in caprine caseinate as well [55].”

• cites [32] 32. Macedo I.Q., Faro C.J., Pires E.V., Caseinolytic specificity of cardosin, an aspartic protease from the cardoon Cynara cardunculus L.: action on bovine α s -and β-casein and comparison with chymosin, J. Agric. Food Chem. 44 (1996) 42-47. sourceSupported
• cites [55] 55. Sousa M.J., Malcata F.X., Proteolysis of ovine and caprine caseins in solution by enzymatic ex- tracts of Cynara cardunculus, Enzyme Microb. Technol. 22 (1998) 305-314. sourceSupported

May combine two claims.

The most susceptible bond on bovine β-casein is Leu192-Tyr193, although proteinases from C. cardunculus were reported to cleave Leu127-Thr128, Leu165-Ser166 and every single peptide bond of Ala189-Tyr193 in bovine β-casein as well.

“The most susceptible bond on bovine β-casein is Leu 192 -Tyr 193 , [32,48], although proteinases from C. cardunculus were reported to cleave Leu 127 -Thr 128 , Leu 165 -Ser 166 and every single peptide bond of Ala 189 -Tyr 193 (i.e.Ala 189 -Phe 190 , Phe 190 -Leu 191 , Leu 191 -Leu 192 and Leu 192 -Tyr 193 ) in bovine β-casein as well [32] (Fig. 1b).”

• cites [32] 32. Macedo I.Q., Faro C.J., Pires E.V., Caseinolytic specificity of cardosin, an aspartic protease from the cardoon Cynara cardunculus L.: action on bovine α s -and β-casein and comparison with chymosin, J. Agric. Food Chem. 44 (1996) 42-47. sourceSupported
• cites [48] 48. Sousa M.J.C.F., Plant rennet substitute from flowers of Cynara cardunculus. MSc thesis, Na- tional University of Ireland, Cork, Ireland, 1993.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

In ovine and caprine caseinates, β-caseins are cleaved at both Leu127-Thr128 and Leu190-Tyr191, but in caprine caseinate the bonds Glu100-Thr101 and Leu136-Pro137 are also broken down.

“In ovine and caprine caseinates, β-caseins (i.e.β 1 -and β 2 -casein, which are two variants that differ in their level of phosphorylation, 6 and 5, respectively) are cleaved at both Leu 127 -Thr 128 and Leu 190 -Tyr 191 , but in caprine caseinate the bonds Glu 100 -Thr 101 and Leu 136 -Pro 137 are also broken down [55] (Fig. 1b).”

• cites [55] 55. Sousa M.J., Malcata F.X., Proteolysis of ovine and caprine caseins in solution by enzymatic ex- tracts of Cynara cardunculus, Enzyme Microb. Technol. 22 (1998) 305-314. sourcePartly supported

  The Experimental data section reports Leu127–Thr128 and Leu190–Tyr191 cleavage in ovine β-casein, and Glu100–Thr101 and Leu127–Thr128 cleavage in caprine β-casein. Its caprine-site list instead gives Pro136–Leu137 and Leu192–Tyr193, so it does not fully support the claimed caprine bond identities. No page number is available in our copy. (LLM, conf=0.85)

  Experimental — accuracy not yet measured

May combine two claims.

The major cleavage site of bovine and ovine κ-casein is Phe105-Met106, whereas caprine κ-casein is preferentially cleaved at Lys116-Thr117.

“The major cleavage site of bovine [31] and ovine κ-casein is Phe 105 -Met 106 , whereas caprine κ-casein is preferentially cleaved at Lys 116 -Thr 117 [55] (Fig. 1a).”

• cites [31] 31. Macedo I.Q., Faro C.J., Pires E.V., Specificity and kinetics of the milk-clotting enzyme from Cardoon (Cynara cardunculus L.) toward bo- vine κ-casein, J. Agric. Food Chem. 41 (1993) 1537-1540. sourceSupported
• cites [55] 55. Sousa M.J., Malcata F.X., Proteolysis of ovine and caprine caseins in solution by enzymatic ex- tracts of Cynara cardunculus, Enzyme Microb. Technol. 22 (1998) 305-314. sourceSupported

May combine two claims.

Comparison of results suggests that the bonds in pure caseins (or in sodium caseinate) most susceptible to cardosins A and B are Leu190-Tyr191 and Leu127-Thr128 in β-casein, and Phe23-Val24 and Trp164-Tyr165 in αs1-casein.

“However, comparison of the results reported by Ramalho-Santos et al. [38,39], by Sousa and Malcata [55], and by Silva and Malcata [46] suggests that the bonds in pure caseins (or in sodium caseinate, for that matter) most susceptible to cardosins A and B are Leu 190 -Tyr 191 and Leu 127 -Thr 128 in β-casein (Fig. 1b), and Phe 23 -Val 24 and Trp 164 -Tyr 165 in α s1 -casein (Fig. 1c).”

• cites [38] 38. Ramalho-Santos M., Veríssimo P., Faro C., Pires E., Action on bovine α s1 -casein of cardosins A and B, aspartic proteinases from the flowers of the cardoon Cynara cardunculus L, Biochim. Biophys. Acta 1297 (1996) 83-89. sourceNot checked — no full text of the source
• cites [39] 39. Ramalho-Santos M., Veríssimo P., Faro C., Pires E., Action on bovine β-casein of cardosins A and B, X Congresso Nacional de Bioquímica, Braga, Portugal, 31st October-2nd November, 1996.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

• cites [55] 55. Sousa M.J., Malcata F.X., Proteolysis of ovine and caprine caseins in solution by enzymatic ex- tracts of Cynara cardunculus, Enzyme Microb. Technol. 22 (1998) 305-314. sourceSupported
• cites [46] 46. Silva S.V., Malcata F.X., On the activity and specificity of cardosin B, a plant proteinase, on ovine caseins, Food Chem. 67 (1999) 373-378. sourceNot checked — no full text of the source

May combine two claims.

Ovine β-casein is degraded by 48.2%, whereas caprine β-casein is degraded by 68.9%, both in caseinate form.

“This is in agreement with Tavaria et al. [60], who reported that ovine β-casein is degraded by 48.2%, whereas caprine β-casein is degraded by 68.9%, both in caseinate form.”

• cites [60] 60. Tavaria F.K., Sousa M.J., Malcata F.X., Storage and lyophilization effects of extracts of Cynara cardunculus on the degradation of ovine and caprine caseins, Food Chem. 72 (2001) 79-88. sourceSupported

May combine two claims.

In solution, the fragment bovine αs1-casein (f24-199) was identified as the major peptide produced by the action of proteinases from C. cardunculus, a result confirmed independently by Macedo et al. [32].

“In solution, the fragment bovine α s1 -casein (f24-199) was identified as the major peptide produced by the action of proteinases from C. cardunculus [48], a result confirmed independently by Macedo et al. [32].”

• cites [48] 48. Sousa M.J.C.F., Plant rennet substitute from flowers of Cynara cardunculus. MSc thesis, Na- tional University of Ireland, Cork, Ireland, 1993.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

• cites [32] 32. Macedo I.Q., Faro C.J., Pires E.V., Caseinolytic specificity of cardosin, an aspartic protease from the cardoon Cynara cardunculus L.: action on bovine α s -and β-casein and comparison with chymosin, J. Agric. Food Chem. 44 (1996) 42-47. sourcePartly supported

  The Results and Discussion identify αs1-casein Phe24–Trp199 as a peptide produced by cardosin, and the proteolysis pathway describes it as a product of the primary cleavage. The paper does not establish that it was the major peptide by abundance in solution; it also describes subsequent cleavage of that fragment. No page number is available in our copy. (LLM, conf=0.82)

  Experimental — accuracy not yet measured

May combine two claims.

Ovine cheeses manufactured from raw milk exhibited higher microbial counts than those from pasteurised milk without starter addition; however, the lowest microbial counts were recorded in cheese with starter added.

“Ovine cheeses manufactured from raw milk exhibited higher microbial counts than those from pasteurised milk without starter addition [51]; however, the lowest microbial counts were recorded in cheese with starter added [7,51].”

• cites [51] 51. Sousa M.J., Malcata F.X., Influence of pasteur- ization of milk and addition of starter cultures on protein breakdown in ovine cheeses manufac- tured with extracts from flowers of Cynara cardunculus, Food Chem. 57 (1996) 549-556. sourceSupported
• cites [7] 7. Carmona M.A., Sanjuan E., Gomez R., Fernandez-Salguero J., Effect of starter cultures on the physico-chemical and biochemical fea- tures in ewe cheese made with extracts from flowers of Cynara cardunculus L., J. Sci. Food Agric. 79 (1999) 737-744. sourceNot checked — no full text of the source

May combine two claims.

In ovine cheese manufactured with C. cardunculus, Phe23-Val24 is already hydrolysed by 7 d, but not before 28 d of ripening when animal coagulant is employed instead.

“In ovine cheese manufactured with C. cardunculus, Phe 23 -Val 24 is already hydrolysed by 7 d, but not before 28 d of ripening when animal coagulant is employed instead.”

May combine two claims.

These bands were produced in ovine milk cheeses from the very beginning of ripening, in caprine milk cheeses after 7 d and in bovine milk cheeses after 28 d, and all became more intense as ripening progressed.

“These bands were produced in ovine milk cheeses from the very beginning of ripening, in caprine milk cheeses after 7 d and in bovine milk cheeses after 28 d, and all became more intense as ripening progressed.”

May combine two claims.

Cardosin A and cardosin B both cleaved bovine αs1-casein at the bonds Phe23-Phe24, Trp164-Tyr165 and Phe153-Tyr154; cardosin A further cleaved the bond Tyr165-Tyr166, whereas cardosin B cleaved in addition the bond Phe150-Arg151.

“Cardosin A and cardosin B both cleaved bovine α s1 -casein at the bonds Phe 23 -Phe 24 , Trp 164 -Tyr 165 and Phe 153 -Tyr 154 ; cardosin A further cleaved the bond Tyr 165 -Tyr 166 , whereas cardosin B cleaved in addition the bond Phe 150 -Arg 151”

May combine two claims.

The maximum activity of extracts of C. cardunculus was obtained via grinding the stylets for 36 s, using an extraction buffer with pH 5.9 without salt, and after homogenisation of the suspension for 15 min.

“The maximum activity of extracts of C. cardunculus was obtained via grinding the stylets for 36 s, using an extraction buffer with pH 5.9 without salt, and after homogenisation of the suspension for 15 min.”

Probably not a substantial claim: may not pass S3 (load-bearing).

Only the stylets and stigmae (violet part) possess a milk-clotting capacity.

“however, it is now accepted that only the stylets and stigmae (violet part) possess a milk-clotting capacity [19,40].”

• cites [19] 19. Faro C.J., Purificação e caracterização físico- química da protease de Cynara cardunculus L. Ph.D. thesis, Universidade de Coimbra, Portu- gal, 1991.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

• cites [40] 40. Ramalho-Santos M., Pissarra J., Verissimo P., Pereira S., Salema R., Pires E., Faro C.J., Cardosin A, an abundant aspartic proteinase, ac- cumulates in protein storage vacuoles in the stig- matic papillae of Cynara cardunculus L., Planta 203 (1997) 204-212. sourceNot checked — no full text of the source

Probably not a substantial claim: may not pass S3 (load-bearing).

Dried flowers of C. cardunculus have been successfully employed for many centuries in the Iberian Peninsula for the manufacture of traditional semi-hard cheeses.

“however, dried flowers of C. cardunculus have been successfully employed for many centuries in the Iberian Peninsula for the manufacture of traditional semi-hard cheeses, i.e. such traditional cheese varieties as Serra da Estrela [1,30,44,65], La Serena (from ewe's milk) [23,36,42], Guía (from a mixture of ewe's and cow's milk) [25] and Los Pedroches (from ewe's milk) [7,24,66].”

• cites [1] 1. Barbosa M., "Cardo" (Cynara cardunculus L.) as vegetable rennet, Boletim do Departamento de Tecnologia e Indústria Alimentar, LNETI- DTIA, Lisboa, Portugal, 1983.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

• cites [30] 30. Macedo A., Malcata F.X., Oliveira J.C., The technology, chemistry, and microbiology of Serra cheese: a review, J. Dairy Sci. 76 (1993) 1725-1739. sourceNot checked — no full text of the source
• cites [44] 44. Roseiro M.L.B., Ewe's milk cheesemaking in Portugal using a vegetable rennet (a review), Sheep Dairy News 8 (1991) 65-80.Not checked — no full text of the source
• cites [65] 65. Vieira-de-Sá F., Barbosa M., Cheese-making experiments with a vegetable rennet from cardo (Cynara cardunculus L.), J. Dairy Res. 39 (1972) 335-343.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

The maximum (estimated) proteolytic activity is obtained after grinding stylets and stigmae for 36 s, using an extraction buffer with pH 5.9 in the absence of salt, and after having homogenised the ground stylets and stigmae in a buffer suspension for 15 min.

“The maximum (estimated) proteolytic activity was obtained after grinding stylets and stigmae for 36 s, using an extraction buffer with pH 5.9 in the absence of salt, and after having homogenised the ground stylets and stigmae in a buffer suspension for 15 min [50].”

• cites [50] 50. Sousa M.J., Malcata F.X., Effects of processing conditions on the caseinolytic activity of pro- teinases from Cynara cardunculus L., Food Sci. Technol. Int. 2 (1996) 255-263.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Extracts of C. cardunculus hydrolyse the insulin B-chain at the carboxylic side of the peptide bond of Phe-X, Leu-X and Ile-X, where X is preferentially Val or Tyr; however, the specificity is not entirely determined by the nature of the residues since Leu11-Val12 of the insulin B-chain was not cleaved.

“Extracts of C. cardunculus were reported to hydrolyse the insulin B-chain at the carboxylic side of the peptide bond of Phe-X, Leu-X and Ile-X, where X was preferentially Val or Tyr; however, the specificity was not entirely determined by the nature of the residues since Leu 11 -Val 12 of the insulin B-chain was not cleaved [20].”

• cites [20] 20. Faro C.J., Moir A.J.G., Pires E.V., Specificity of a milk clotting enzyme extracted from the thistle Cynara cardunculus L.: Action on oxidised in- sulin and κ-casein, Biotechnol. Lett. 14 (1992) 841-846. sourceNot checked — no full text of the source

May combine two claims.

The drying process decreases the proteolytic activity, especially that of cardosin B, and thus has a considerable effect on the observed overall proteolytic activity.

“The drying process decreases the proteolytic activity, especially that of cardosin B (which is the stronger enzyme in the crude extract), and thus has a considerable effect on the observed overall proteolytic activity [17].”

• cites [17] 17. Esteves C., Estudo comparativo das características bioquímicas dos coalhos de Cynara cardunculus L., Cynara scolymus L., e Cynara humilis L. MSc thesis, Universidade de Coimbra, Portugal, 1995.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Cardosin A is similar to chymosin, whereas cardosin B resembles pepsin.

“it was thus shown that cardosin A is similar to chymosin, whereas cardosin B resembles pepsin.”

• cites [63] 63. Veríssimo P., Esteves C., Faro C., Pires E., The vegetable rennet of Cynara cardunculus L. con- tains two proteinases with chymosin and pepsin- like specificities, Biotechnol. Lett. 17 (1995) 621-626.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Those proteinases have a pH optimum of 5.1 and are classified as aspartic proteinases.

“Those proteinases were reported to have a pH optimum of 5.1 and they were classified as aspartic proteinases [27].”

• cites [27] 27. Heimgartner U., Pietrzak M., Geertsen R., Brodelius P., Silva Figueiredo A.C., Pais M.S.S., Purification and partial characterization of milk clotting proteases from flowers of Cynara cardunculus, Phytochemistry 29 (1990) 1405- 1410. sourceNot checked — no full text of the source

Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.

Very few aspartic proteinases from plant origin have been isolated and partially characterised to date; one of their unique features is an extra segment of ca. 100 amino acids, which bears no sequence similarity with aspartic proteinases of mammalian or microbial origin.

“Very few aspartic proteinases from plant origin have been isolated and partially characterised to date [59]; one of their unique features is an extra segment of ca. 100 amino acids, which bears no sequence similarity with aspartic proteinases of mammalian or microbial origin [21].”

• cites [59] 59. Tavaria F., Sousa M.J., Domingos A., Malcata F.X., Brodelius P., Clemente A., Pais M.S., Deg- radation of caseins from milk of different species by extracts of Centaurea calcitrapa, J. Agric. Food Chem. 45 (1997) 3760-3765. sourceNot checked — no full text of the source
• cites [21] 21. Faro C.J., Veríssimo P., Lin Y., Tang J., Pires E.V., in: Takahashi K. (Ed.), Aspartic protein- ases: Structure, Function, Biology and Biomed- ical Implications, Plenum Press, New York, USA, 1995, pp. 373-377.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.

Each cardosin occurs in dimeric form, with apparent molecular masses of 31 and 15 kg.mol-1 for the monomers of cardosin A, and 34 and 14 kg.mol-1 for those in cardosin B.

“These authors also reported that each cardosin occurs in dimeric form, with apparent molecular masses of 31 and 15 kg .mol -1 for the monomers of cardosin A, and 34 and 14 kg .mol -1 for those in cardosin B.”

• cites [63] 63. Veríssimo P., Esteves C., Faro C., Pires E., The vegetable rennet of Cynara cardunculus L. con- tains two proteinases with chymosin and pepsin- like specificities, Biotechnol. Lett. 17 (1995) 621-626.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Only two of the three original peaks (peaks 2 and 3) possessed clotting and proteolytic activities; these two proteinases were later named cardosin A (peak 2) and cardosin B (peak 3).

“Sousa [48] indicated that only two of the three original peaks (peaks 2 and 3) possessed clotting and proteolytic activities; these two proteinases were later named cardosin A (peak 2) and cardosin B (peak 3) [63].”

• cites [48] 48. Sousa M.J.C.F., Plant rennet substitute from flowers of Cynara cardunculus. MSc thesis, Na- tional University of Ireland, Cork, Ireland, 1993.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

• cites [63] 63. Veríssimo P., Esteves C., Faro C., Pires E., The vegetable rennet of Cynara cardunculus L. con- tains two proteinases with chymosin and pepsin- like specificities, Biotechnol. Lett. 17 (1995) 621-626.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

Probably not a substantial claim: may not pass S3 (load-bearing).

Flowers of C. cardunculus contain one acid proteinase with two glycosylated sub-units, with molecular masses of 31 and 16 kg.mol-1.

“Flowers of C. cardunculus were claimed to contain one acid proteinase with two glycosylated sub-units, with molecular masses of 31 and 16 kg .mol -1 ; that enzyme was found to induce milk coagulation through cleavage of the Phe 105 -Met 106 bond in bovine κ-casein [20].”

• cites [20] 20. Faro C.J., Moir A.J.G., Pires E.V., Specificity of a milk clotting enzyme extracted from the thistle Cynara cardunculus L.: Action on oxidised in- sulin and κ-casein, Biotechnol. Lett. 14 (1992) 841-846. sourceNot checked — no full text of the source

May combine two claims.

The peptide bond Leu192-Tyr193 in bovine β-casein is the most susceptible to hydrolysis by cardosin A or cardosin B, but the bonds Leu127-Thr128 and Leu165-Ser166 are also cleaved.

“The peptide bond Leu 192 -Tyr 193 in bovine β-casein was reported to be the most susceptible to hydrolysis by cardosin A or cardosin B, but the bonds Leu 127 -Thr 128 and Leu 165 -Ser 166 were also cleaved [39].”

• cites [39] 39. Ramalho-Santos M., Veríssimo P., Faro C., Pires E., Action on bovine β-casein of cardosins A and B, X Congresso Nacional de Bioquímica, Braga, Portugal, 31st October-2nd November, 1996.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Cardosin A cleaves insulin B-chain at the bonds Leu15-Tyr16, Leu17-Val18 and Phe25-Try26, whereas cardosin B also cleaves Glu13-Ala14, Ala14-Leu15 and Phe24-Phe25, thus implying a broader specificity for the latter.

“Later, cardosin A was reported to cleave insulin B-chain at the bonds Leu 15 -Tyr 16 , Leu 17 -Val 18 and Phe 25 -Try 26 , whereas cardosin B also cleaved Glu 13 -Ala 14 , Ala 14 -Leu 15 and Phe 24 -Phe 25 , thus implying a broader specificity for the latter [63].”

• cites [63] 63. Veríssimo P., Esteves C., Faro C., Pires E., The vegetable rennet of Cynara cardunculus L. con- tains two proteinases with chymosin and pepsin- like specificities, Biotechnol. Lett. 17 (1995) 621-626.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Cardosin A cleaves ovine caseinate at the bonds Phe105-Met106 of ovine κ-casein, Leu127-Thr128, Leu165-Ser166 and Leu190-Tyr191 of ovine β-casein, and Trp164-Tyr165 of ovine αs1-casein.

“Cardosin A cleaved ovine caseinate at the bonds Phe 105 -Met 106 of ovine κ-casein, Leu 127 -Thr 128 , Leu 165 -Ser 166 and Leu 190 -Tyr 191 of ovine β-casein, and Trp 164 -Tyr 165 of ovine α s1 -casein [45]”

• cites [45] 45. Silva S.V., Malcata F.X., On the use of reversed- phase HPLC to characterize the specificity of cardosins from Cynara cardunculus toward ovine caseins, XXVII Scientific Meeting of Chromatography, Lugo, Spain, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

Probably not a substantial claim: may not pass S3 (load-bearing).

Proteolysis by cardosin A is faster than by cardosin B.

“proteolysis by cardosin A was reported to be faster than by cardosin B [47].”

• cites [47] 47. Silva S.V., Malcata F.X., Comparative catalytic action of two plant proteinases upon caprine ca- seins in solution, Food Chem. 71 (2000) 207-214. sourceNot checked — no full text of the source

Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.

The bonds Leu165-Ser166 and Trp164-Tyr165 are the most susceptible to cardosin B when this enzyme acts upon isolated ovine β- and αs1-caseins, respectively.

“The bonds Leu 165 -Ser 166 and Trp 164 -Tyr 165 were reported by Silva and Malcata [46] to be the most susceptible to cardosin B when this enzyme acted upon isolated ovine βand α s1 -caseins, respectively.”

• cites [46] 46. Silva S.V., Malcata F.X., On the activity and specificity of cardosin B, a plant proteinase, on ovine caseins, Food Chem. 67 (1999) 373-378. sourceNot checked — no full text of the source

May combine two claims.

Cardosin B cleaves ovine β-casein at three primary sites, viz. Leu127-Thr128, Leu165-Ser166 and Leu190-Tyr191, and ovine αs1-casein at two primary sites, viz. Leu156-Asp157 and Trp164-Tyr165.

“cardosin B cleaved ovine β-casein at three primary sites, viz.Leu 127 -Thr 128 , Leu 165 -Ser 166 and Leu 190 -Tyr 191 , and ovine α s1 -casein at two primary sites, viz.Leu 156 -Asp 157 and Trp 164 -Tyr 165 [46].”

• cites [46] 46. Silva S.V., Malcata F.X., On the activity and specificity of cardosin B, a plant proteinase, on ovine caseins, Food Chem. 67 (1999) 373-378. sourceNot checked — no full text of the source

May combine two claims.

Ratio of hydrophobic to hydrophilic peptides decreases consistently during ripening in bovine and caprine cheeses, attaining 15.0 and 7.3, respectively, by end of ripening; in ovine cheese, this ratio goes through a maximum by 14 d and decreases thereafter to reach 29.9 by 68 d.

“The ratio of hydrophobic to hydrophilic peptides (Tab.I) decreased consistently during ripening in bovine and caprine cheeses, hence attaining 15.0 and 7.3, respectively, by the end of ripening; however, this ratio went through a maximum by 14 d in ovine cheese and decreased thereafter to reach 29.9 by 68 d of ripening [49].”

• cites [49] 49. Sousa M.J.C.F., Characterization of the proteolytic action of the flowers of Cynara cardunculus in ovine, caprine and bovine cheeses. Ph.D. thesis, Escola Superior de Biotecnologia, Porto, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Percent degradation of bovine αs1-casein is 86% by 68 d of ripening, whereas degradation levels in the αs-casein region are 47% in ovine and 86% in caprine milk cheeses.

“Sousa and Malcata [52] found that the percent degradation of bovine α s1 -casein is 86% by 68 d of ripening, whereas the bands with highest mobility (i.e.those designated as the α s -casein region) exhibit degradation levels of 47% and 86% in ovine and caprine milk cheeses, respectively (Fig. 3).”

• cites [52] 52. Sousa M.J., Malcata F.X., Comparative bio- chemical evolution during ripening of bovine, ovine and caprine cheeses manufactured with extracts of flowers of Cynara cardunculus, Z. Lebensm. Unters. Forsch. 205 (1997) 97-103.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Concentration of hydrophobic peptides increases up to 68 d of ripening in caprine cheese, and up to 14 d in bovine and ovine cheeses, but apparently decreases thereafter.

“The concentration of hydrophobic peptides (Tab.I) increased up to 68 d of ripening in caprine cheese, and up to 14 d in bovine and ovine cheeses, but apparently decreased thereafter”

• cites [49] 49. Sousa M.J.C.F., Characterization of the proteolytic action of the flowers of Cynara cardunculus in ovine, caprine and bovine cheeses. Ph.D. thesis, Escola Superior de Biotecnologia, Porto, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Degradation of αs-caseins decreases as NaCl content increases, yielding 86% for bovine and caprine cheeses and 46% for ovine cheeses containing ca. 2.1% or 3.0% NaCl, respectively.

“The degradation of α s -caseins (again assessed by densitometry) decreased as the NaCl content increased (to yield 86% for bovine and caprine cheeses, and 46% for ovine cheeses, containing ca. 2.1% or 3.0% NaCl, respectively) [49], in agreement with results by Noomen [35] for Meshanger-type cheese, and Delacroix and Trossat [15] for Gruyère-type cheeses.”

• cites [49] 49. Sousa M.J.C.F., Characterization of the proteolytic action of the flowers of Cynara cardunculus in ovine, caprine and bovine cheeses. Ph.D. thesis, Escola Superior de Biotecnologia, Porto, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

• cites [35] 35. Noomen A., Activity of proteolytic enzymes in simulated soft cheeses (Meshanger type). 2. Ac- tivity of calf rennet, Neth. Milk Dairy J. 32 (1978) 26-48.Not checked — no full text of the source
• cites [15] 15. Delacroix-Buchet A., Trossat P., Proteolysis and texture of Gruyere type cheeses. 1. Influence of water activity, Lait 71 (1991) 299-311.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Degradation of bovine β-casein is 33%, and that of combined β1- and β2-caseins is 33% in ovine and 43% in caprine milk cheeses.

“Degradation of bovine β-casein was 33%, and that of combined β 1 -and β 2 -caseins was 33% and 43% in ovine and caprine milk cheeses, respectively (Fig. 3) [52].”

• cites [52] 52. Sousa M.J., Malcata F.X., Comparative bio- chemical evolution during ripening of bovine, ovine and caprine cheeses manufactured with extracts of flowers of Cynara cardunculus, Z. Lebensm. Unters. Forsch. 205 (1997) 97-103.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

At early ripening, WSN/TN differs significantly between ovine cheese and caprine cheese (8.28%) (P=0.03) and between ovine and bovine cheese (6.59%) (P=0.01), but not between caprine and bovine cheeses (P=0.10).

“Statistically significant differences (on the 5% level) were found for WSN/TN between ovine cheese and either caprine (8.28%) (P = 0.03) or bovine (6.59%) (P = 0.01) cheeses, at early ripening, but no statistically significant differences were found between caprine and bovine cheeses (P = 0.10) [49].”

• cites [49] 49. Sousa M.J.C.F., Characterization of the proteolytic action of the flowers of Cynara cardunculus in ovine, caprine and bovine cheeses. Ph.D. thesis, Escola Superior de Biotecnologia, Porto, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

By 68 d of ripening, WSN/TN is significantly higher for caprine (48.7%) and ovine (46.4%) than for bovine (32.9%) cheeses, and caprine and ovine cheeses differ significantly from one another (P<0.0001).

“These authors also showed that, by 68 d of ripening, WSN/TN was significantly higher for caprine (48.7%) (P < 0.0001) and ovine (46.4%) (P < 0.0001) than for bovine (32.9%) cheeses; however, caprine and ovine cheeses were significantly different from one another (P < 0.0001).”

• cites [49] 49. Sousa M.J.C.F., Characterization of the proteolytic action of the flowers of Cynara cardunculus in ovine, caprine and bovine cheeses. Ph.D. thesis, Escola Superior de Biotecnologia, Porto, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Concentration of hydrophilic peptides increases up to 68 d of ripening in ovine and caprine cheeses, and up to 56 d in bovine cheese.

“ripening in ovine and caprine cheeses, and up to 56 d in bovine cheese [49].”

• cites [49] 49. Sousa M.J.C.F., Characterization of the proteolytic action of the flowers of Cynara cardunculus in ovine, caprine and bovine cheeses. Ph.D. thesis, Escola Superior de Biotecnologia, Porto, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

In Cheddar cheese, reduction in fat level results in greater degradation of β-casein; concentration of intact β-casein in full fat and low fat Cheddar cheeses after 180 d of ripening were ca. 90% and 58%, respectively.

“In Cheddar cheese manufactured with milk standardised to different fat contents, reduction in the fat level resulted in greater degradation of β-casein; the concentration of intact β-casein in the full fat and low fat Cheddar cheeses after 180 d of ripening were ca.90% and 58%, respectively [22].”

• cites [22] 22. Fenelon M.A., Guinee T.P., Primary proteolysis and textural changes during ripening in Cheddar 168 M.J. Sousa, F.X. Malcata cheese manufactured to different fat contents, Int. Dairy J. 10 (2000) 151-158. sourceNot checked — no full text of the source

May combine two claims.

γ-caseins arising from degradation of β-casein by plasmin increase in concentration throughout ripening of bovine cheeses, but cannot be identified in WISF of either ovine or caprine cheeses.

“The γ -caseins (i.e.γ 1 -, γ 2 -and γ 3 -caseins) arising from degradation of the β-casein by plasmin [68] increased in concentration throughout ripening of bovine cheeses, but could not be identified in the WISF of either ovine or caprine cheeses [49].”

• cites [68] 68. Visser S., Proteolytic enzymes and their action on milk proteins (a review), Neth. Milk Dairy J. 35 (1981) 65-88.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

• cites [49] 49. Sousa M.J.C.F., Characterization of the proteolytic action of the flowers of Cynara cardunculus in ovine, caprine and bovine cheeses. Ph.D. thesis, Escola Superior de Biotecnologia, Porto, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Proteinases from C. cardunculus (like most coagulants) and, probably to a lesser extent, plasmin hydrolyse caseins down to large- and intermediate-size peptides, which are then broken down by residual coagulant, as well as by proteinases and peptidases from starter and nonstarter bacteria.

“The proteinases from C. cardunculus (like those of most coagulants) and, probably to a lesser extent, plasmin hydrolyse caseins down to large-and intermediate-size peptides, which are then broken down by residual coagulant, as well as by proteinases and peptidases from starter and nonstarter bacteria.”

May combine two claims.

The most susceptible bond of β-casein has been cleaved, so the complementary fragment should be β-casein (f1-192) in bovine β-casein, or β-casein (f1-190) in ovine and caprine β-casein.

“β-casein (f191-) in ovine and caprine cheeses (Tab.III), confirmed that the most susceptible bond of β-casein has been cleaved, so the complementary fragment should be the peptide β-casein (f1-192) (a) in bovine β-casein, or β-casein (f1-190) (d and g) in ovine and caprine β-casein, respectively.”

May combine two claims.

The main hydrolysis sites associated with C. cardunculus coagulant action are Leu127-Thr128, Leu165-Ser166 and Leu192-Tyr193 in bovine β-casein, Leu127-Thr128 and Leu190-Tyr191 in ovine β-casein, and Leu127-Thr128 and Leu190-Tyr191 in caprine β-casein.

“The main hydrolysis sites identified in association with said coagulant action were Leu 127 -Thr 128 , Leu 165 -Ser 166 and Leu 192 -Tyr 193 in bovine β-casein, Leu 127 -Thr 128 and Leu 190 -Tyr 191 in ovine β-casein [56], and Leu 127 -Thr 128 and Leu 190 -Tyr 191 in caprine β-casein.”

• cites [56] 56. Sousa M.J., Malcata F.X., Identification of pep- tides from ovine milk cheese manufactured with animal rennet or extracts of Cynara cardunculus as coagulant, J. Agric. Food Chem. 46 (1998) 4034-4041. sourceNot checked — no full text of the source

May combine two claims.

Caseins from bovine, ovine and caprine milk share relatively similar amino acid sequences, implying that they should be similarly hydrolysed in the same susceptible regions.

“Caseins from the three types of milk share relatively similar amino acid sequences (Fig. 1a-d), thus implying that they should be similarly hydrolysed in the (same) susceptible regions.”

May combine two claims.

Sousa [49] sequenced peptides β-casein (f128-), β-casein (f166-) and β-casein (f193-) from bovine β-casein, and β-casein (f128-) and β-casein (f191-) from ovine and caprine β-casein, which were probably produced by plant proteinases of interest.

“Sousa [49] sequenced the peptides β-casein (f128-), β-casein (f166-) and β-casein (f193-) from bovine β-casein (Tab.III), and β-casein (f128-) and β-casein (f191-) from ovine and caprine β-casein (Tab.III), which were probably produced by the plant proteinases of interest.”

• cites [49] 49. Sousa M.J.C.F., Characterization of the proteolytic action of the flowers of Cynara cardunculus in ovine, caprine and bovine cheeses. Ph.D. thesis, Escola Superior de Biotecnologia, Porto, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Proteinases from C. cardunculus (and also chymosin) have been implicated in the formation of bitter peptides in cheese, so factors that affect retention and activity of coagulant in the curd influence development of bitterness.

“Proteinases from C. cardunculus (and also chymosin) have been implicated in the formation of bitter peptides in cheese, so factors that affect retention (and also activity) of coagulant in the curd will surely influence development of bitterness.”

May combine two claims.

Formation of hydrophobic peptides in cheese manufactured with plant coagulant proceeds for a longer time than in cheese manufactured with chymosin; highest level of hydrophobic peptides occurs by 24 h of ripening when plant coagulant is employed, ca. two-fold that found with chymosin.

“Gaya et al. [26] reported that the formation of hydrophobic peptides in cheese manufactured with plant coagulant proceeded for a longer time than in cheese manufactured with chymosin; these authors also pointed out the highest level of hydrophobic peptides by 24 h of ripening when plant coagulant was employed, which was ca.two-fold that found in cheese manufactured with chymosin.”

• cites [26] 26. Gaya P., Carrera E., Medina M., Nuñez M., For- mation of hydrophobic peptides during the man- ufacture of ewe's milk Manchego cheese using different milk coagulants, Milchwissenchaft 54 (1999) 556-558.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Several peptide fragments were reported in bovine, ovine and caprine β-casein, but only a few could be traced as having been released by coagulant proteinases.

“Several peptide fragments were reported in bovine, ovine and caprine β-casein (Tab.III) [49], but only a few could be traced as having been released by coagulant proteinases.”

• cites [49] 49. Sousa M.J.C.F., Characterization of the proteolytic action of the flowers of Cynara cardunculus in ovine, caprine and bovine cheeses. Ph.D. thesis, Escola Superior de Biotecnologia, Porto, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Extracts of C. cardunculus or C. humilis have no appreciable effect on bulk composition, but extracts of C. humilis resulted in higher lactic acid content and higher pH values than cheeses produced with C. cardunculus.

“Vioque et al. [66] reported that extracts of C. cardunculus or C. humilis have no appreciable effect on bulk composition, but extracts of the latter resulted in higher lactic acid content and higher pH values than in those cheeses produced with C. cardunculus.”

• cites [66] 66. Vioque M., Gómez R., Sánchez E., Mata C., Tejada L., Fernández-Salguero J., Chemical and microbiological characteristics of ewe's milk cheese manufactured with extracts from flowers of Cynara cardunculus and Cynara humilis, J. Agric. Food Chem. 48 (2000) 451-456. sourceNot checked — no full text of the source

May combine two claims.

Microbiological viable counts (total, coliforms and lactobacilli) were similar in cheeses produced with both types of plant coagulant, although enterobacteria, yeasts and moulds were found at higher viable numbers in cheese produced with C. humilis than with C. cardunculus.

“Those authors reported that microbiological viable counts (total, coliforms and lactobacilli) were similar in cheeses produced with both types of plant coagulant, although enterobacteria, yeasts and moulds were found at higher viable numbers in cheese produced with C. humilis than with C. cardunculus.”

• cites [66] 66. Vioque M., Gómez R., Sánchez E., Mata C., Tejada L., Fernández-Salguero J., Chemical and microbiological characteristics of ewe's milk cheese manufactured with extracts from flowers of Cynara cardunculus and Cynara humilis, J. Agric. Food Chem. 48 (2000) 451-456. sourceNot checked — no full text of the source

Probably not a substantial claim: may not pass S3 (load-bearing), S4 (based).

The fact that in Cheddar and Camembert the bond Phe23-Val24 is rapidly hydrolysed is probably due to the larger amounts of animal rennet added.

“the fact that in Cheddar and Camembert the bond Phe 23 -Val 24 is rapidly hydrolysed is probably due to the larger amounts of animal rennet added”

May combine two claims.

WSN was higher in cheeses manufactured with extracts of C. cardunculus than with C. humilis, but WSN in cheeses with C. humilis was much higher than in Los Pedroches cheese manufactured with chymosin.

“Vioque et al. [66] showed that WSN was higher in cheeses manufactured with extracts of C. cardunculus than with C. humilis, but WSN in cheeses with C. humilis was much higher than in Los Pedroches cheese manufactured with chymosin [24].”

• cites [66] 66. Vioque M., Gómez R., Sánchez E., Mata C., Tejada L., Fernández-Salguero J., Chemical and microbiological characteristics of ewe's milk cheese manufactured with extracts from flowers of Cynara cardunculus and Cynara humilis, J. Agric. Food Chem. 48 (2000) 451-456. sourceNot checked — no full text of the source
• cites [24] 24. Fernández-Salguero J., Sanjuán E., Influence of vegetable and animal rennet on proteolysis dur- ing ripening in ewe's milk cheese, Food Chem. 64 (1999) 177-183. sourceNot checked — no full text of the source

May combine two claims.

Proteolysis in cheese manufactured with these extracts is associated mainly with the action of this rennet rather than with the prevailing microflora or otherwise adventitious enzymes, and proceeds to a high extent but a low degree.

“Proteolysis in cheese manufactured with these extracts is associated mainly with the action of this rennet rather than with the prevailing microflora or otherwise adventitious enzymes, and proceeds to a high extent but a low degree.”

May combine two claims.

The type of coagulant has no significant effect upon cheese bulk chemical composition throughout ripening, and no significant microbiological differences were detected between cheeses manufactured with C. cardunculus or animal rennet.

“Comparing averages and 95% confidence intervals, it has been stated [53] that the type of coagulant has no significant effect upon cheese bulk chemical composition throughout ripening, and that no significant microbiological differences were detected between cheeses manufactured with C. cardunculus or animal rennet.”

• cites [53] 53. Sousa M.J., Malcata, F.X., Comparison of plant and animal rennets in terms of microbiological, chemical and proteolysis characteristics of ovine cheese, J. Agric. Food Chem. 45 (1997) 74-81. sourceNot checked — no full text of the source

Probably not a substantial claim: may not pass S3 (load-bearing).

The electrophoretic patterns of the WISF of both cheeses unfold a higher susceptibility of αs- than β-casein to proteolysis.

“The electrophoretic patterns of the WISF of both cheeses were claimed to unfold a higher susceptibility of α s -than β-casein to proteolysis [24,36,53].”

• cites [24] 24. Fernández-Salguero J., Sanjuán E., Influence of vegetable and animal rennet on proteolysis dur- ing ripening in ewe's milk cheese, Food Chem. 64 (1999) 177-183. sourceNot checked — no full text of the source
• cites [36] 36. Núñez M., Fernández-del-Pozo B., Rodríguez- Marin M.A., Gaya, P., Medina M., Effect of veg- etable and animal rennet on chemical, microbio- logical, rheological and sensory characteristics of La Serena cheese, J. Dairy Res. 58 (1991) 511-519. sourceNot checked — no full text of the source
• cites [53] 53. Sousa M.J., Malcata, F.X., Comparison of plant and animal rennets in terms of microbiological, chemical and proteolysis characteristics of ovine cheese, J. Agric. Food Chem. 45 (1997) 74-81. sourceNot checked — no full text of the source

May combine two claims.

Cheeses manufactured with plant coagulant exhibited significantly higher levels of WSN/TN; that coagulant had significantly less proteolytic activity upon αs and β-caseins than animal rennet.

“Cheeses manufactured with plant coagulant exhibited significantly higher levels of WSN/TN; that coagulant had significantly less proteolytic activity upon α sand β-caseins than animal rennet [53].”

• cites [53] 53. Sousa M.J., Malcata, F.X., Comparison of plant and animal rennets in terms of microbiological, chemical and proteolysis characteristics of ovine cheese, J. Agric. Food Chem. 45 (1997) 74-81. sourceNot checked — no full text of the source

May combine two claims.

The peptides β-casein (f128-), β-casein (f166-) and β-casein (f191-) were produced by plant rennet only, whereas β-casein (f164-) and β-casein (f191-) were produced by animal rennet only.

“The peptides β-casein (f128-), β-casein (f166-) and β-casein (f191-) were produced by plant rennet only, whereas β-casein (f164-) and β-casein (f191-) were produced by animal rennet only [56].”

• cites [56] 56. Sousa M.J., Malcata F.X., Identification of pep- tides from ovine milk cheese manufactured with animal rennet or extracts of Cynara cardunculus as coagulant, J. Agric. Food Chem. 46 (1998) 4034-4041. sourceNot checked — no full text of the source

May combine two claims.

The peptide αs1-casein (f24-165) is present only in ovine cheese manufactured with C. cardunculus, whereas the peptide αs1-casein (f120-191) was only produced by animal rennet.

“These bands were identified as the peptide α s1 -casein (f24-165), which is present only in ovine cheese manufactured with C. cardunculus, whereas the peptide α s1casein (f120-191) was only produced by animal rennet [56].”

• cites [56] 56. Sousa M.J., Malcata F.X., Identification of pep- tides from ovine milk cheese manufactured with animal rennet or extracts of Cynara cardunculus as coagulant, J. Agric. Food Chem. 46 (1998) 4034-4041. sourceNot checked — no full text of the source

Classified as probably not a substantial claim.

Identical conditions, including standardised amounts of plant and animal coagulants, were employed.

“note that identical conditions, including standardised amounts of plant and animal coagulants, were employed”

May combine two claims.

The water-soluble fraction of pasteurised milk cheeses with starter addition showed differences by long ripening times relative to raw milk cheeses and pasteurised milk cheeses without starter addition; furthermore, a higher number of peptides was present in pasteurised milk cheeses with starter addition.

“However, their WSF showed differences by long ripening times for pasteurised milk cheeses with starter addition relative to raw milk cheeses and pasteurised milk cheeses without starter addition; furthermore, a higher number of peptides was present in pasteurised milk cheeses with starter addition [49].”

• cites [49] 49. Sousa M.J.C.F., Characterization of the proteolytic action of the flowers of Cynara cardunculus in ovine, caprine and bovine cheeses. Ph.D. thesis, Escola Superior de Biotecnologia, Porto, Portugal, 1998.Not matched

  Couldn’t be matched to a paper in Crossref, so it can’t be checked.

May combine two claims.

Significant effects of the breed source of milk were observed with respect to the ripening index (WSN/TN); higher proteolysis was recorded in ovine and caprine than in bovine cheeses.

“Significant effects of the breed source of milk were observed with respect to the ripening index (WSN/TN); higher proteolysis was recorded in ovine and caprine than in bovine cheeses.”

May combine two claims.

Pasteurisation and addition of starter cultures have no appreciable effect on the characteristics of the cheeses throughout ripening; nevertheless, differences were found between the cheeses in terms of WSN/TN, as well as between cheeses manufactured from pasteurised milk with or without starter addition, in terms of TCASN and PTASN.

“Pasteurisation and addition of starter cultures have no appreciable effect on the characteristics of the cheeses throughout ripening; nevertheless, differences were found between the cheeses in terms of WSN/TN, as well as between cheeses manufactured from pasteurised milk with or without starter addition, in terms of TCASN and PTASN.”

Probably not a substantial claim: may not pass S4 (based). May combine two claims.

Cardosin A is similar to chymosin, and cardosin B is similar to chymosin, in terms of their specificity and kinetic parameters.

“cardosin A was claimed to be similar to chymosin, whereas cardosin B was claimed to be similar to chymosin, in terms of their specificity and kinetic parameters.”

May combine two claims.

Proteinases of C. cardunculus produced higher levels of the ripening index than commercial animal rennet, even though the former led to lower levels of the ripening depth index (TCASN/TN) and the free amino acid index (PTASN/TN).

“Proteinases of C. cardunculus produced higher levels of the ripening index than commercial animal rennet, even though the former led to lower levels of the ripening depth index (TCASN/TN) and the free amino acid index (PTASN/TN).”