Proteolysis in Irish farmhouse Camembert cheese during ripening
Open accessAbstract
Proteolysis in an Irish farmhouse Camembert cheese was studied during 10 weeks of ripening. Urea-polyacrylamide gel electrophoresis of pH 4.6-insoluble fractions of cheese showed the degradation of caseins, initially due to the action of chymosin and plasmin and later due to Penicillium camemberti proteinases. Proteolytic specificities of Penicillium camemberti proteinases on the caseins in milk hydrolysates were determined and 64, 6, 28, and 2 cleavage sites were identified in αs1-, αs2-, β-, and κ-casein, respectively. Proteolysis in cheese was studied and peptides produced were determined and compared to the cleavage specificities of Penicillium camemberti proteinases. Regions most susceptible to proteolysis were 1–40, 79–114, and 168–199 in αs1-casein; 42–79 and 97–116 in αs2-casein; 40–57, 101–125, 143–189, and 165–209 in β-casein; and 31–81 and 124–137 in κ-casein. The present study describes in detail the proteolytic action of proteinases from Penicillium camemberti in Camembert cheese during ripening. Practical applications Camembert cheese is a major international cheese variety, made in many countries around the world. The ripening of the cheese involves many biochemical changes and this study provides new information on peptides produced during ripening. Penicillium camemberti is an important mold used in the production of this type of cheese and detailed information is provided on the action of its enzymes on the caseins. Data reported in this study furthers the understanding of the ripening of Camembert cheese.
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- Findingown data
Penicillium camemberti proteinases had 64, 6, 28, and 2 cleavage sites in αs1-, αs2-, β-, and κ-casein, respectively, in milk hydrolysates.
“Proteolytic specificities of Penicillium camemberti proteinases on the caseins in milk hydrolysates were determined and 64, 6, 28, and 2 cleavage sites were identified in α -, α -, β-, and κcasein, respectively.”
Quote in the paperSubstantial claim - Findingown data
Total amino acid contents of 1997 and 3048 μg/g of cheese were found at 6 and 10 weeks, respectively.
“Total amino acid contents of 1997 and 3,048 µg/g of cheese were found at 6 and 10 weeks, respectively, indicating extensive proteolysis.”
Quote in the paperSubstantial claim - Findingown data
Levels of pH 4.6-SN/TN increased from 12.90% to 25.64% during ripening.
“Levels of pH 4.6-SN/TN increased from 12.90% to 25.64% (Table 1), indicating extensive proteolysis during ripening.”
Quote in the paperSubstantial claim - Findingown data
Extensive breakdown of αs1- and β-casein was observed in electrophoretograms from 6 weeks onward.
“Extensive breakdown of α -and β-casein was observed in electrophoretograms from 6 weeks onward, in agreement with earlier studies (Sousa & McSweeney, 2001).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Sousa & McSweeney, 2001
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Findingown data
Peptides eluting later (hydrophobic) from 27 to 45 min were at higher concentration early in ripening (2 days, MLD and WRP) as compared to late ripening.
“Peptides eluting later (hydrophobic) from 27 to 45 min were at higher concentration early in ripening (2 days, MLD and WRP) as compared to late ripening.”
Quote in the paperNot a substantial claim
- Findingown data
Production of a large number of peptides as a result of proteolysis was observed from UPLC chromatograms of pH 4.6-soluble extracts.
“Production of a large number peptides as a result of proteolysis was observed from the UPLC chromatograms of the pH 4.6-soluble extracts (Figure 2).”
Quote in the paperNot a substantial claim - Findingown data
Hydrolyzates produced from centrifuged culture filtrates at the end of growth contained a large number of peptides produced by the proteolytic action of mold proteinases on the caseins.
“Hydrolyzates produced from centrifuged culture filtrates (potato dextrose broth + 10% LHSMP) at the end of the growth, contained a large number of peptides produced by the proteolytic action of mold proteinases on the caseins (Figure 4)”
Quote in the paperSubstantial claim- Rests on an assumption: Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
- Findingown data
Concentration of all individual amino acids was higher at 10 weeks than at 6 weeks.
“Concentration of all individual amino acids was observed to be higher at 10 weeks than at 6 weeks.”
Quote in the paperNot a substantial claim - Findingown data
Fat content showed no significant difference during ripening.
“likewise there was no significant difference in % fat.”
Quote in the paperNot a substantial claim - Findingown data
pH values showed a significant increase over the 10-week ripening (4.9-7.3).
“pH values showed a significant increase over the 10-week ripening (4.9-7.3).”
Quote in the paperSubstantial claim - Findingown data
Certain regions of the caseins were more susceptible to proteolysis by mold proteinases from culture hydrolyzates: αs1-casein residues 1-42, 79-96, and 101-145; αs2-casein residues 100-125; β-casein residues 34-59, 110-130, and 145-204.
“Regions that were most susceptible to the action of mold proteinases from the culture hydrolyzates in α -casein were from residues 1-42, 79-96, and 101-145; in α -casein were from residues 100-125; in β-casein were from residues 34-59, 110-130, and 145-204.”
Quote in the paperSubstantial claim- Rests on an assumption: Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
- Findingown data
Lactocepin-derived peptide fragment αs1-CN (f28-34), produced by cleavage at Pro-Phe, was found at all time points of ripening.
“Lactocepinderived peptide fragment α -CN (28-34), produced by cleavage at Pro -Phe , is a reported bioactive peptide, with casokinin 7-ACE inhibitory activity (Sun & Jenssen, 2012), and was found at all the time points of ripening.”
Quote in the paperNot a substantial claim - Findingown data
Major cleavage sites of P. camemberti proteinases identified in β-casein were Gln-Ser, Gln-Asp, Lys-Glu, Pro-Phe, Trp-Met, Met-His, Lys-Val, Phe-Leu, Tyr-Gln, Gln-Glu, and Pro-Val.
“in β-casein were Gln -Ser , Gln -Asp , Lys -Glu , Pro -Phe , Trp -Met , Met -His , Lys -Val , Phe -Leu , Tyr -Gln , Gln -Glu and Pro -Val ;”
Quote in the paperSubstantial claim - Findingown data
Composition and pH4.6-SN/TN showed a significant difference after 4 weeks of ripening.
“Composition and pH4.6-SN/TN showed a significant difference after 4 weeks of ripening indicating action of mold enzymes and extensive proteolysis.”
Quote in the paperSubstantial claim - Findingnone given
Fragments produced by the action of PC-proteinases, plasmin, and lactocepins at their N-termini were αs1-CN (f115-125) and αs1-CN (f115-126).
“Fragments produced by the action of PC-proteinases, plasmin, and lactocepins at their N-termini were α -CN (f115-125) and α -CN (f115-126).”
Quote in the paperNot a substantial claim - Findingown data
In αs2-casein, PC proteinases cleaved at sites Leu-Tyr, Tyr-Gln, Gln-Gly, Arg-Asn, Pro-Ile and Lys-Leu.
“In case of α -casein (Figure 5b), PC proteinases cleaved at sites Leu -Tyr , Tyr -Gln , Gln -Gly , Arg -Asn , Pro -Ile and Lys -Leu .”
Quote in the paperSubstantial claim- Rests on an assumption: Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
- Findingown data
β-CN (f192-206) was found at all time points of ripening.
“The peptide fragment was found at all the time points of ripening (Supplementary Data Table S2).”
Quote in the paperNot a substantial claim - Findingown data
Major cleavage sites of P. camemberti proteinases identified in αs1-casein were Glu-Val, Arg-Leu, Leu-His, His-Ser, and Phe-Ser.
“Major cleavage sites of P. camemberti proteinases identified in α -casein were Glu -Val , Arg -Leu , Leu -His , His -Ser , Phe -Ser ;”
Quote in the paperSubstantial claim - Findingown data
In β-casein, PC proteinases cleaved at sites Gln-Ser, Gln-Asp, Lys-Glu, Pro-Phe, Trp-Met, Met-His, Lys-Val, Phe-Leu, Tyr-Gln, Gln-Glu and Pro-Val.
“In β-casein (Figure 5c), PC proteinases cleaved at sites Gln -Ser , Gln -Asp , Lys -Glu , Pro -Phe , Trp -Met , Met -His , Lys -Val , Phe -Leu , Tyr -Gln , Gln -Glu and Pro -Val .”
Quote in the paperSubstantial claim- Rests on an assumption: Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
- Findingown data
The regions from which most peptides were derived in αs1-casein were residues 42-79 and 97-116.
“The regions from which most peptides were derived in α -casein (Figure 6b), were from residues 42-79 and 97-116 (Figure 6b).”
Quote in the paperNot a substantial claim - Findingreasoning
The common fragment αs1-CN (f1-23) produced by the action of chymosin was absent at all stages of ripening.
“The common fragment, α -CN (f1-23) produced by the action of chymosin (Fox & McSweeney, 1996), was absent at all stages of ripening.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Fox & McSweeney, 1996 source
- Findingown data
Urea-PAGE, UPLC, and LC-MS analyses provide qualitative and quantitative differences in cheese during 10-week ripening.
“Urea-PAGE, UPLC, and LC-MS analyses provide qualitative and quantitative differences in cheese during 10-week ripening.”
Quote in the paperSubstantial claim - Findingown data
Major peptide fragments identified were αs1-CN (f14-23), αs1-CN (f17-23/24), αs1-CN (f24-34), and αs1-CN (f25-34).
“Major peptide fragments identified were α -CN (f14-23), α -CN (f17-23/24), α -CN (f 24-34), and α -CN (f 25-34).”
Quote in the paperNot a substantial claim - Findingown data
pH 4.6-soluble nitrogen increased during 10-week ripening of Irish farmhouse Camembert cheese.
“The current study investigated proteolysis with in Camembert cheese respect levels of pH 4.6-soluble nitrogen that increased during 10-week ripening.”
Quote in the paperSubstantial claim - Findingown data
Major cleavage sites of P. camemberti proteinases identified in αs2-casein were Leu-Tyr, Tyr-Gln, Gln-Gly, Arg-Asn, Pro-Ile, and Lys-Leu.
“in α -casein were Leu -Tyr , Tyr -Gln , Gln -Gly , Arg -Asn , Pro -Ile and Lys -Leu”
Quote in the paperSubstantial claim - Findingcitation
Cleavage sites in common between P. roqueforti PR-R and P. camemberti proteinases in αs1-casein were Leu-Asn, Lys-Val, Glu-Pro, Ser-Glu, Tyr-Leu, Arg-Leu, His-Ser, Leu-Asp and Lys-Thr.
“Cleavages sites in common between enzymes from the mold species in α -casein were Leu -Asn , Lys -Val , Glu -Pro , Ser -Glu , Tyr -Leu , Arg -Leu , His -Ser Leu -Asp and Lys -Thr”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Mane et al., 2019 source
- Findingcitation
Fragments produced from pH 4.6-soluble extract by action of lactocepins at their N- or C-terminus were κ-CN (f31-41), κ-CN (f60-80), κ-CN (f71-82), κ-CN (f72-84), and κ-CN (f102-111), produced by cleavage at Tyr-Val, Pro-Tyr, Pro-Ala, Ala-Gln, and Pro-His.
“Fragments produced from pH 4.6-soluble extract, by action of lactocepins at their N-or C-terminus (Ardo et al., 2017) were κ-CN (f31-41), κ-CN (f60-80), κ-CN (f71-82), κ-CN (f72-84), and κ-CN (f102-111), produced by cleavage at Tyr -Val , Pro -Tyr , Pro -Ala , Ala -Gln and Pro -His .”
Quote in the paperNot a substantial claim - Findingcitation
Plasmin and PC proteinases both cleaved β-casein at sites Lys-Glu and Arg-Asp.
“Plasmin (Ardo et al., 2017) and PC proteinases both cleaved at sites Lys -Glu and Arg -Asp .”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Ardo et al., 2017 source
- Rests on an assumption: Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
- Findingcitation
Cleavage sites common to PC proteinases and chymosin in αs1-casein were Phe-Phe, Phe-Val, Met-Glu, Lys-His, His-Ile, Lys-Tyr, Lys-Val and Asp-Ile.
“Cleavage sites common to action of both PC proteinases and chymosin (Ardo et al., 2017) in α -casein (Figure 5a) were Phe -Phe , Phe -Val , Met -Glu , Lys -His , His -Ile , Lys -Tyr , Lys -Val and Asp -Ile .”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Ardo et al., 2017 source
- Rests on an assumption: Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
- Findingown data
In κ-casein, regions most susceptible to proteolysis were residues 31-81 and 124-137.
“Regions most susceptible to proteolysis were from residues 31-81 and 124-137 (Figure 6d).”
Quote in the paperNot a substantial claim - Findingcitation
Sites cleaved by lactocepins and PC proteinases in αs1-casein were Gln-Glu, Leu-Asn and Phe-Gly.
“Sites cleaved by the action lactocepins (Ardo et al., 2017) and PC proteinases were Gln -Glu , Leu -Asn and Phe -Gly”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Ardo et al., 2017 source
- Rests on an assumption: Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
- Findingcitation
Cleavage sites common to PC proteinases, chymosin, and lactocepins in αs1-casein were Gln-Glu, Phe-Phe and Phe-Gly.
“Cleavage sites in common to action of PC proteinases, chymosin, and lactocepins (Fox & McSweeney, 1996) in α -casein were Gln -Glu , Phe -Phe and Phe -Gly .”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Fox & McSweeney, 1996 source
- Rests on an assumption: Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
- Findingown data
Major αs1-casein fragments produced during ripening were derived from residues 1-40, 79-114, and 168-199.
“Major α -casein (Figure 6a) fragments produced during ripening were derived from residues 1-40, 79-114, and 168-199 (Figure 6a).”
Quote in the paperNot a substantial claim - Findingcitation
The β-casein cleavage sites Lys-Val, Lys-Glu and Lys-Ile were also identified in this study.
“these cleavage sites were also identified in this study.”
Quote in the paperNot a substantial claim - Findingown data
In β-casein, regions most susceptible to proteolysis were residues 40-57, 101-125, 143-189, and 165-209.
“In case of β-casein, regions that were most susceptible to proteolysis were from residues 40-57, 101-125, 143-189, and 165-209 (Figure 6c).”
Quote in the paperSubstantial claim - Findingcitation
In β-casein, P. roqueforti PR-R and PC proteinases both cleaved at sites Asn-Glu, Leu-Pro, Val-Tyr and Tyr-Val.
“In case of β-casein, PR-R and PC proteinases both cleaved at sites Asn -Glu , Leu -Pro , Val -Tyr and Tyr -Val .”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Mane et al., 2019 source
- Findingown data
A small number of peptides from κ-caseins was found in low concentrations during ripening.
“A small number of peptides from κ-caseins (Figure 6d), was found in low concentrations during ripening.”
Quote in the paperNot a substantial claim - Findingown data
The only cleavage sites for PC proteinases in κ-casein were at Pro-Pro and Pro-Glu.
“The only cleavage sites for PC proteinases in κ-casein (Figure 5d) were at Pro -Pro and Pro -Glu .”
Quote in the paperNot a substantial claim- Rests on an assumption: Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
- Findingown data
Major cleavage sites in αs1-casein produced by PC proteinases were Glu-Val, Arg-Leu, Leu-His, His-Ser and Phe-Ser.
“Major cleavage sites in α -casein produced by the action of PC proteinases were Glu -Val , Arg -Leu , Leu -His , His -Ser and Phe -Ser .”
Quote in the paperSubstantial claim- Rests on an assumption: Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
- Findingown data
A large number of peptides was produced during ripening.
“A large number of peptides was produced during ripening (Supplementary Data Table S2).”
Quote in the paperNot a substantial claim - Findingcitation
Fragments αs1-CN (f80-88), αs1-CN (f150-161/162), αs1-CN (f151-156/158/161/162/163), and αs1-CN (f196-208) were found in Camembert at all stages of ripening.
“Action of plasmin and lactocepins (Ardo et al., 2017) on α -casein helped to produce fragments α -CN (f80-88), α -CN (f150-161/162), α -CN (f151-156/158/161/162/163), and α -CN (f196-208), which were also found in Camembert at all stages of ripening (Table 2).”
Quote in the paperNot a substantial claim - Findingown data
Major cleavage sites of P. camemberti proteinases identified in κ-caseins were Pro-Pro and Pro-Glu.
“and in κ-caseins were Pro -Pro and Pro -Glu .”
Quote in the paperSubstantial claim - Interpretationown data
The difference in the concentrations of amino acids between 6- and 10-week cheese samples indicated extensive proteolysis.
“The difference in the concentrations of amino acids between 6-and 10-week cheese samples indicated extensive proteolysis.”
Quote in the paperSubstantial claim - Interpretationown data
In the Irish farmhouse Camembert, degradation of caseins in pH 4.6-insoluble fractions occurred initially due to chymosin and plasmin and later due to Penicillium camemberti proteinases.
“Urea-polyacrylamide gel electrophoresis of pH 4.6-insoluble fractions of cheese showed the degradation of caseins, initially due to the action of chymosin and plasmin and later due to Penicillium camemberti proteinases.”
Quote in the paperSubstantial claim - Interpretationown data
The complexity of the chromatograms indicated a high number of peptides.
“The complexity of the chromatograms indicated a high number of peptides.”
Quote in the paperNot a substantial claim - Interpretationreasoning
The peptides were progressively hydrolyzed from 4 weeks and later time points of ripening, probably due to the combined effect of aspartyl and metalloproteinases.
“The peptides were progressively hydrolyzed from 4 weeks and later time points of ripening, probably due to the combined effect of aspartyl and metalloproteinases.”
Quote in the paperSubstantial claim - Interpretationcitation
The moisture values found are typical for Camembert cheese.
“values found are typical for this variety of cheese”
Quote in the paperNot a substantial claim0 of 3 sources checked- cites Guizani et al., 2002 source
- cites Khidr, 1995
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- cites Sousa & McSweeney, 2001
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Premisecitation
Levels of free amino acids tend to increase with ripening of Camembert cheese.
“Levels of free amino acids also tend to increase with ripening of Camembert cheese (Bergamini, Hynes, & Zalazar, 2006;Tejada, Abellan, Cayuela, Martinez-Cacha, & Fernandez-Salguero, 2008), which is in agreement with the current results.”
Quote in the paperNot a substantial claim0 of 2 sources checked - Interpretationown data
The increase in pH 4.6-SN/TN indicates extensive proteolysis during ripening.
“Levels of pH 4.6-SN/TN increased from 12.90% to 25.64% (Table 1), indicating extensive proteolysis during ripening.”
Quote in the paperSubstantial claim - Interpretationreasoning
Less complexity at later time points suggested degradation of peptides into very short peptides or free amino acids which have early elution times.
“Less complexity at later time points suggested degradation of peptides into very short peptides or free amino acids which have early elution times.”
Quote in the paperNot a substantial claim - Interpretationown data
The total amino acid contents indicate extensive proteolysis.
“Total amino acid contents of 1997 and 3,048 µg/g of cheese were found at 6 and 10 weeks, respectively, indicating extensive proteolysis.”
Quote in the paperSubstantial claim - Interpretationreasoning
The absence of αs1-CN (f1-23) is likely due to action of cell envelope-associated proteinases or lactocepins and endopeptidases of starter and nonstarter bacteria, which can hydrolyze αs1-casein.
“The reason for this is likely the action of cell envelope-associated proteinases or lactocepins and endopeptidases of starter and nonstarter bacteria, which can hydrolyze α”
Quote in the paperSubstantial claim - Interpretationcitation
Peptide fragment αs1-CN (f148-161) produced by cleavage at Phe-Thr is a bioactive peptide with angiotensin-converting enzyme (ACE) inhibitory activity.
“Likewise, peptide fragment α -CN (f148-161) produced by cleavage at Phe -Thr is a bioactive peptide (Table 2) with angiotensinconverting enzyme (ACE) inhibitory activity, (Sistla, 2013).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Sistla, 2013 source
- Premisecitation
κ-CN (f96-105) was produced by chymosin cleaving at its C-terminus (Phe-Met).
“κ-CN (f96-105) was produced by chymosin cleaving at its C-terminus (Phe -Met ); (Ardo et al., 2017).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Ardo et al., 2017 source
- Interpretationown data
The hydrolysis of αs1-CN (f1-23) at its N-terminal bonds is likely due to the action of cell envelope-associated proteinases or lactocepins and endopeptidases of starter and nonstarter bacteria.
“likely the action of cell envelope-associated proteinases or lactocepins and endopeptidases of starter and nonstarter bacteria, which can hydrolyze α -CN(f1-23) rapidly (Figure 1) at the N-terminal bonds”
Quote in the paperSubstantial claim - Premisecitation
β-CN (f108-124) is produced by cleavage at sites common to action of PC proteinases and plasmin.
“These susceptible regions of the casein resulted in one fragment, β-CN (f108-124) produced by cleavage at sites common to action of PC proteinases and plasmin (Ardo et al., 2017;Fox et al., 1994).”
Quote in the paperNot a substantial claim0 of 2 sources checked- cites Ardo et al., 2017 source
- cites Fox et al., 1994
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Premisecitation
Peptide fragments β-CN (f47-52/55/56), β-CN (f191-204), and β-CN (f194-206) are derived from action of PC proteinases and lactocepins at their N- or C-termini.
“Peptide fragments derived from action of PC proteinases and lactocepins at their N-or C-termini (Ardo et al., 2017) were β-CN (f47-52/55/56), β-CN (f191-204), and β-CN (f194-206).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Ardo et al., 2017 source
- Interpretationcitation
Peptides produced during ripening were mainly due to the action of plasmin and lactocepins.
“Peptides produced during ripening were mainly due to the action of plasmin and lactocepins (Ardo et al., 2017).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Ardo et al., 2017 source
- Premisecitation
Action of plasmin and lactocepins on αs1-casein produces fragments αs1-CN (f80-88), αs1-CN (f150-161/162), αs1-CN (f151-156/158/161/162/163), and αs1-CN (f196-208).
“Action of plasmin and lactocepins (Ardo et al., 2017) on α -casein helped to produce fragments α -CN (f80-88), α -CN (f150-161/162), α -CN (f151-156/158/161/162/163), and α -CN (f196-208), which were also found in Camembert at all stages of ripening (Table 2).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Ardo et al., 2017 source
- Premisecitation
PC proteinases hydrolyzed Lys-Val, Lys-Glu and Lys-Ile faster than other bonds in β-casein.
“Trieu-Cuot, Archieri-Haze, and Gripon (1982) showed that PC proteinases hydrolyzed Lys -Val , Lys -Glu and Lys -Ile faster than other bonds in β-casein; these cleavage sites were also identified in this study.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Trieu-Cuot, Archieri-Haze, and Gripon (1982) source
- Interpretationnone given
The αs2-casein sites Leu-Tyr, Tyr-Gln, Gln-Gly, Arg-Asn, Pro-Ile and Lys-Leu are not known to be cleaved by plasmin or lactocepin.
“These sites are not known to be cleaved by plasmin or lactocepin.”
Quote in the paperSubstantial claim - Premisecitation
Peptides produced by action of lactocepins and/or chymosin at their N- or C-termini include αs1-CN (f30-38), αs1-CN (f31-37/38), αs1-CN (f33-40), αs1-CN (f154-164), αs1-CN (f165-193), αs1-CN (f169-189/190/197/198), αs1-CN (f170-189/190/192/198), and αs1-CN (f180-198/199).
“Peptides produced by action of lactocepins and/or chymosin at their N-or C-termini (Ardo et al., 2017) included α -CN (f30-38), α -CN (f31-37/38), α -CN (f33-40), α -CN (f154-164), α -CN (f165-193), α -CN (f169-189/190/197/198), α -CN (f170-189/190/192/198), and α -CN (f180 -198/199).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Ardo et al., 2017 source
- May combine two claims. 15
- Classified as probably not a substantial claim. 15
May combine two claims.
Findingown dataCrude protein and %N values of cheese showed a significant increase (12.66%-18.15% and 1.99%-2.84%, respectively).
“Crude protein and %N values of cheese showed a significant increase (12.66%-18.15% and 1.99%-2.84%,respectively).”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
FindingcitationThe pH 4.6-SN/TN values in the current study were slightly higher than the ~18% values of the outer part of the same Irish Camembert cheese studied at 4 weeks by Sousa and McSweeney (2001).
“Reported values from the current study were slightly higher than the values (~18%) of the outer part of the same Irish Camembert cheese studied at 4 weeks by Sousa and McSweeney (2001).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Sousa & McSweeney, 2001
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
May combine two claims.
Findingown dataMoisture levels in the Irish farmhouse Camembert were ~55%-59% and did not increase significantly over 10 weeks of ripening.
“Moisture levels (~55%-59%) showed no significant increase as ripening proceeded”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown dataRegions most susceptible to proteolysis in the cheese were 1-40, 79-114, and 168-199 in αs1-casein; 42-79 and 97-116 in αs2-casein; 40-57, 101-125, 143-189, and 165-209 in β-casein; and 31-81 and 124-137 in κ-casein.
“Regions most susceptible to proteolysis were 1-40, 79-114, and 168-199 in α -casein; 42-79 and 97-116 in α -casein; 40-57, 101-125, 143-189, and 165-209 in β-casein; and 31-81 and 124-137 in κ-casein.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
FindingcitationThe crude protein and %N values were similar to those reported earlier.
“These values were similar to those reported earlier (Sousa & McSweeney, 2001)”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Sousa & McSweeney, 2001
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
May combine two claims.
Findingown dataNaCl content was almost the same throughout ripening (1.66%-1.77%) with no significant increase.
“The % NaCl was almost same throughout ripening (1.66%-1.77%),with no significant increase”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown dataPeptide fragments β-CN (f47-52/55/56), β-CN (f191-204), and β-CN (f194-206) were found from wrapping stage to end of ripening.
“These peptide fragments were found from wrapping stage to end of the ripening.”
Quote in the paperNot a substantial claimMay combine two claims.
Findingown dataA large number of peptides derived from αs1-casein were observed as this protein was strongly degraded throughout cheese ripening.
“A large number of peptides derived from α -casein were observed as this protein was strongly degraded throughout cheese ripening.”
Quote in the paperNot a substantial claimMay combine two claims.
InterpretationcitationBreakdown of β-caseins into γ-caseins by plasmin was observed on electrophoretograms of Camembert, and plasmin action was favored by the high pH of the cheese.
“Breakdown of β-caseins into γ-caseins by the action of plasmin was observed on electrophoretograms of Camembert; plasmin action was favored by the high pH of the cheese (Figure 1; Gripon, 1993;Trieu-Cuot & Gripon, 1982).”
Quote in the paperNot a substantial claim0 of 2 sources checkedProbably not a substantial claim: may not pass S3 (load-bearing).
InterpretationcitationResults of previous studies on Camembert are in agreement with the concentrations of free amino acids found in the present work.
“Results of previous studies on Camembert (Boutrou et al., 1999(Boutrou et al., , 2006;;Boutrou & Guéguen, 2005;Guizani et al., 2002;Lee & Bae, 2018;Mei, Guo, Wu, Li, & Yu, 2015;Sousa & McSweeney, 2001) are in agreement with the concentrations of free amino acids found in the present work.”
Quote in the paperNot a substantial claim0 of 3 sources checkedMay combine two claims.
PremisecitationpH 4.6-SN/TN is commonly used as an index of proteolysis, and in Camembert this fraction is mainly produced by chymosin, plasmin, lactocepins and mold proteinases acting on the caseins.
“pH 4.6-SN/TN (%) is commonly used as an index of proteolysis and this fraction is mainly produced in Camembert by the action of chymosin, plasmin, lactocepins (LacCeps) and proteinases from the mold on the caseins”
Quote in the paperSubstantial claim0 of 2 sources checked- cites Gripon, Desmazeaud, Lebars, & Bergere, 1975
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- cites Guizani et al., 2002 source
Classified as probably not a substantial claim.
Premisenone givenProteolysis during ripening of Camembert cheese is catalyzed by chymosin, plasmin, starter proteinases, peptidases, and mold (aspartyl, metallo-) proteinases.
“Proteolysis during ripening of Camembert cheese is catalyzed by chymosin, plasmin, starter proteinases, peptidases, and mold (aspartyl, metallo-) proteinases.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
InterpretationcitationOverall, the gross composition was typical of Camembert cheese.
“Overall, the gross composition was observed to be typical of Camembert cheese (Guizani et al., 2002;Sousa & McSweeney, 2001).”
Quote in the paperNot a substantial claim0 of 2 sources checked- cites Guizani et al., 2002 source
- cites Sousa & McSweeney, 2001
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
May combine two claims.
InterpretationcitationThe significant increase in proteolysis begins at the surface of the cheese at MLD (day 6 of ripening) and is mainly associated with action of chymosin and plasmin up to 4 weeks and later also due to P. camemberti proteinases from 6 weeks onward.
“The significant increase in proteolysis begins at the surface of the cheese at MLD (day 6 of ripening) (Boutrou et al., 1999;Boutrou & Guéguen, 2005;Boutrou, Kerriou, & Gassi, 2006;Guizani et al., 2002), and is mainly associated with action of chymosin and plasmin up to 4 weeks and later also due to P. camemberti proteinases from 6 weeks onward.”
Quote in the paperSubstantial claim0 of 3 sources checkedMay combine two claims.
InterpretationcitationThe increase in pH during ripening results from metabolism of lactic acid and release of NH3 due to deamination of free amino acids, both caused by action of the mold.
“The increase in pH during ripening results from metabolism of lactic acid, release of NH due to deamination of free amino acids, both caused by action of the mold (Grippon, 1993).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Grippon, 1993
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
May combine two claims.
PremisecitationThe increase in pH was slow initially but pH of the interior rapidly equilibrated with the outer part after 30 days.
“The increase was slow initially but pH of the interior rapidly equilibrated with the outer part after 30 days (Sousa & McSweeney, 2001).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Sousa & McSweeney, 2001
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).
InterpretationcitationResults for Camembert were similar to the amino acid profiles of blue cheeses.
“Results for Camembert were similar to the amino acid profiles of blue cheeses (Mane et al., 2019;Zarmpoutis, McSweeney, & Fox, 1997).”
Quote in the paperNot a substantial claim0 of 2 sources checked- cites Mane et al., 2019 source
- cites Zarmpoutis, McSweeney, & Fox, 1997
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).
PremisecitationHigh concentrations of lysine, leucine, valine, phenylalanine, and proline have previously been found in Camembert.
“High concentrations of lysine, leucine, valine, phenylalanine, and proline have previously been found in Camembert (Kubiková & Grouch, 1998).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Kubiková & Grouch, 1998
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.
InterpretationcitationHigh concentration of glutamic acid in Camembert and other mold ripened cheeses can be explained by its presence in high quantities in caseins or by production from α-ketoglutarate by action of aminotransferases.
“High concentration of glutamic acid in Camembert and other mold ripened cheeses can be explained by its presence in high quantities in caseins or by production from α-ketoglutarate by action of aminotranferases (Vicente, Ibàñez, Barcina, & Barron, 2001).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Vicente, Ibàñez, Barcina, & Barron, 2001 source
Probably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductnone givenOnly peptides derived from the caseins were considered.
“Only peptides derived from the caseins were considered.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Premisecitationαs1-CN (f28-34) is a reported bioactive peptide with casokinin-7 ACE inhibitory activity.
“Lactocepinderived peptide fragment α -CN (28-34), produced by cleavage at Pro -Phe , is a reported bioactive peptide, with casokinin 7-ACE inhibitory activity (Sun & Jenssen, 2012), and was found at all the time points of ripening.”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Sun & Jenssen, 2012 source
May combine two claims.
InterpretationcitationCertain regions in a casein were highly susceptible to enzymatic hydrolysis and contained common cleavage sites for PC-proteinases, chymosin, and lactocepins.
“Certain regions in a casein were highly susceptible to enzymatic hydrolysis and contained common cleavage sites for PC-proteinases, chymosin, and lactocepins (Ardo et al., 2017).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Ardo et al., 2017 source
Probably not a substantial claim: may not pass S3 (load-bearing).
Premisecitationβ-CN (f192-206) is a bioactive peptide fragment with casecidin-15 antimicrobial activity.
“A bioactive peptide fragment derived from the action lactocepins at its N-terminus, β-CN (f192-206) (Table 2), produced by cleavage at Leu -Leu ; this peptide possesses casecidin-15 antimicrobial activity (Rizzello et al., 2005).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Rizzello et al., 2005 source
May combine two claims.
InterpretationcitationAction of PC proteinases produced peptide fragment αs1-CN (f80-89) by cleavage at Lys-His; this peptide is known to have antioxidant activity.
“Action of PC proteinases produced peptide fragment α -CN (f80-89) produced by cleavage at Lys -His ; this peptide is known to have antioxidant activity (Table 2) (Baum, Fedorova, Ebner, Hoffmann, & Pischetsrieder, 2013).”
Quote in the paperNot a substantial claim0 of 1 sources checked- cites Baum, Fedorova, Ebner, Hoffmann, & Pischetsrieder, 2013
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).
Study design and conductnone givenExperimental analysis was repeated in triplicate for each sample.
“Experimental analysis were repeated in triplicate for each sample and data were analyzed using R© 16 (R version 3.4.0; the R foundation for Statistical Computing, University of Auckland, New Zealand).”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductown dataMass spectra were searched with a false discovery rate of 1% on the peptide level.
“Mass spectra were searched using the default setting of MaxQuant namely a false discovery rate of 1% on the peptide level.”
Quote in the paperNot a substantial claimMay combine two claims.
Interpretationown dataThe significant difference in composition and pH4.6-SN/TN after 4 weeks indicates action of mold enzymes and extensive proteolysis.
“Composition and pH4.6-SN/TN showed a significant difference after 4 weeks of ripening indicating action of mold enzymes and extensive proteolysis.”
Quote in the paperSubstantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductown dataCheeses were obtained from three separate batches.
“Whole Irish farmhouse Camembert cheeses, manufactured according to the traditional cheese-making procedure of the manufacturer were obtained frozen from the manufacturer (300 g) from three separate batches were at 2 days, molding (MLD) at 4 days, wrapping (WRP) at ~2, 4, 6, 8, and 10 weeks of ripening.”
Quote in the paperNot a substantial claimProbably not a substantial claim: may not pass S3 (load-bearing).
Study design and conductnone givenDifferences in means between samples were tested by one-way ANOVA at a significance level of .05 throughout the study.
“Differences in means between the samples were tested by (one-way ANOVA) analysis of variance at significance level, a, of .05(P value ≤.05), throughout the study.”
Quote in the paperNot a substantial claim
The paper relies on this without support.
Detailed specificities of Penicillium camemberti proteinases on the caseins are unknown.
“However, detailed specificities of proteinases from Penicilium camemberti (PC proteinases) on the caseins are unknown.”
The paper relies on this without support.
Very little has been reported in the literature about generation of peptides during the ripening of this particular variety of cheese.
“Very little has been so far been reported in the literature about generation of peptides during the ripening of this particular variety of cheese, which is commercially very important.”
The paper relies on this without support.
The proteolytic specificities of P. camemberti proteinases determined in culture filtrates are representative of their action in Camembert cheese.
“Peptides identified were compared with cleavage specificities of PC proteinases determined earlier and with known specificities of chymosin, plasmin, and lactocepins”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The rise in pH is a consequence of the activity of P. candidum PCA1/TT031 that metabolizes lactic acid and lactate and causes the breakdown of curd components.
“Which is a consequence of the activity of P. candidum PCA1/TT031 that metabolizes lactic acid and lactate (Kaminaries et al. 2019; Mane and McSweeney 2020) and causes the breakdown of curd components.”
From Optimizing the acceleration of Cheddar cheese ripening using response surface methodology by microbial protease without altering its quality features (2021) · cites this paper as Mane and McSweeney 2020
Section 3.1, “Compositional analysis,” reports that pH rose during ripening and attributes the rise partly to the mold’s metabolism of lactic acid. Section 3.3 reports that Penicillium camemberti proteinases break down caseins. The paper does not identify the mold as P. candidum PCA1/TT031 or establish these effects for that specific strain. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Antioxidant peptide has conflicting residue endpoints
MinorThe results identify the antioxidant peptide as residues 80-89 and point to Table 2, which lists its fragment as 80-90.
“Action of PC proteinases produced peptide fragment α -CN (f80-89) produced by cleavage at Lys -His ; this peptide is known to have antioxidant activity (Table 2)”
“| α -CN | HIQKEDVPSER | Antioxidant | Milk | 80-90 | Baum et al. (2013) |”
Salt's reported lack of a significant increase conflicts with Table 1
MinorSalt rises from 1.66% at wrapping to 1.77% at four weeks; Table 1 assigns those values different significance groups, a and b.
“The % NaCl was almost same throughout ripening (1.66%-1.77%),with no significant increase”
“| WRP | 5.06 ± 0.01 | a | 58.01 ± 0.59 | a | 28.17 ± 0.58 | a | 1.66 ± 0.07 | a | 2.09 ± 0.06 | a | | 4 w | 6.00 ± 0.14 | b | 55.95 ± 1.38 | a | 31.83 ± 0.29 | c | 1.77 ± 0.02 | b | 2.30 ± 0.03 | b |”
Fat is described as having no significant differences despite table groupings
MinorTable 1 places wrapping-stage fat in group a and four-week fat in group c, contrary to the statement that fat did not differ significantly.
“likewise there was no significant difference in % fat.”
“| WRP | 5.06 ± 0.01 | a | 58.01 ± 0.59 | a | 28.17 ± 0.58 | a | 1.66 ± 0.07 | a | 2.09 ± 0.06 | a | | 4 w | 6.00 ± 0.14 | b | 55.95 ± 1.38 | a | 31.83 ± 0.29 | c | 1.77 ± 0.02 | b | 2.30 ± 0.03 | b |”
Molding is dated both four and six days into ripening
MinorThe sample description identifies molding (MLD) as day 4, whereas the results identify MLD as day 6.
“The significant increase in proteolysis begins at the surface of the cheese at MLD (day 6 of ripening)”
“at 2 days, molding (MLD) at 4 days, wrapping (WRP)”
Moisture is described as unchanged despite a significant 10-week increase
MinorThe text says moisture did not increase significantly, but Table 1 assigns the 10-week value group b and the earlier values group a, indicating a significant difference.
“Moisture levels (~55%-59%) showed no significant increase as ripening proceeded”
“| 8 w | 7.05 ± 0.11 | c | 56.08 ± 1.12 | a | 30.17 ± 0.58 | bc | 1.75 ± 0.01 | ab | 2.71 ± 0.09 | cd | | 10 w 7.33 ± 0.04 | c | 59.45 ± 0.43 | b | 31.83 ± 0.29 | c | 1.75 ± 0.01 | ab | 2.84 ± 0.09 | d | |”
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“Mass spectra were searched using the default setting of MaxQuant namely a false discovery rate of 1% on the peptide level.”
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“Results of previous studies on Camembert (Boutrou et al., 1999, 2006; Boutrou & Guéguen, 2005; Guizani et al., 2002; Lee & Bae, 2018; Mei, Guo, Wu, Li, & Yu, 2015; Sousa & McSweeney, 2001) are in agreement with the concentrations of free amino acids found in the present work.”
BackgroundResultProteolysis in Cheese during Ripening
Upadhyay, V. K., McSweeney, P. L. H., Magboul, A. A. A., & Fox, P. F. (2004) · Cheese · doi:10.1016/s1874-558x(04)80076-9 · Cited by 206 · see citing works
Self-citationAntibacterial Activities of Peptides from the Water-Soluble Extracts of Italian Cheese Varieties
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Self-citationPotentiometric Determination of Salt in Cheese
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BackgroundMethodInfluentialBiochemistry of Cheese Ripening: Proteolysis
Ardö, Y., McSweeney, P. L. H., Magboul, A. A. A., Upadhyay, V. K., & Fox, P. F. (2017) · Cheese · doi:10.1016/b978-0-12-417012-4.00018-1 · Cited by 121 · cited 18× · see citing works
“Action of plasmin and lactocepins (Ardo et al., 2017) on αs2-casein helped to produce fragments αs2-CN (f80–88), αs2-CN (f150–161/162), αs2-CN (f151–156/158/161/162/163), and αs2-CN (f196–208), which were also found in Camembert at all stages of ripening (Table 2).”
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Identification of ACE-inhibitory peptides in different Spanish cheeses by tandem mass spectrometry
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BackgroundInfluentialContribution of Geotrichum candidum to the proteolysis of soft cheese
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Changes in the composition of juice expressed from Camembert cheese during ripening
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“Results of previous studies on Camembert (Boutrou et al., 1999, 2006; Boutrou & Guéguen, 2005; Guizani et al., 2002; Lee & Bae, 2018; Mei, Guo, Wu, Li, & Yu, 2015; Sousa & McSweeney, 2001) are in agreement with the concentrations of free amino acids found in the present work.”
BackgroundResultProteolysis in Danish blue cheese during ripening
Mane, A., Ciocia, F., Beck, T. K., Lillevang, S. K., & McSweeney, P. L. H. (2019) · International Dairy Journal · doi:10.1016/j.idairyj.2019.05.017 · Cited by 40 · cited 3× · see citing works
“Results for Camembert were similar to the amino acid profiles of blue cheeses (Mane et al., 2019; Zarmpoutis, McSweeney, & Fox, 1997).”
ResultInfluentialSelf-citationInfluence of cheese-making recipes on the composition and characteristics of Camembert-type cheese
Batty, D., Waite-Cusic, J. G., & Meunier‐Goddik, L. (2018) · Journal of Dairy Science · doi:10.3168/jds.2018-14964 · Cited by 37 · see citing works
Role of Penicillium roqueforti proteinases during blue cheese ripening
Bars, D. L., & Gripon, J. C. (1981) · Journal of Dairy Research · doi:10.1017/s0022029900021968 · Cited by 36 · see citing works
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Guizani, N., Kasapis, S., Al-Attabi, Z. H., & Al-Ruzeiki, M. H. (2002) · International Journal of Food Properties · doi:10.1081/jfp-120015486 · Cited by 32 · see citing works
Trieu-Cuot, P., Archieri-Haze, M.-J., & Gripon, J.-C. (1982) · Journal of Dairy Research · doi:10.1017/s0022029900022627 · Cited by 32 · cited 1× · see citing works
“Breakdown of β-caseins into γ-caseins by the action of plasmin was observed on electrophoretograms of Camembert; plasmin action was favored by the high pH of the cheese (Figure 1; Gripon, 1993; Trieu-Cuot, Archieri-Haze, and Gripon, 1982).”
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“Both aspartyl proteinase and metalloproteinase are synthesized and their levels in cheese are maximal after about 15 days and then decrease slowly (Lenoir, 1984; Spinnler, 2017).”
BackgroundInfluentialIdentification of the Principal Water-insoluble Peptides in Cheddar Cheese
Mooney, J. S., Fox, P. F., Healy, A., & Leaver, J. (1998) · International Dairy Journal · doi:10.1016/s0958-6946(98)00116-2 · Cited by 31 · see citing works
Comparison of the level of residual coagulant activity in different cheese varieties
Bansal, N., Fox, P. F., & McSweeney, P. L. H. (2009) · Journal of Dairy Research · doi:10.1017/s0022029909004075 · Cited by 30 · see citing works
Self-citationFernández, M., Singh, T. K., & Fox, P. F. (1998) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf9710950 · Cited by 29 · see citing works
Structure–activity relationships of αs-casein peptides with multifunctional biological activities
Sistla, S. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1778-4 · Cited by 28 · cited 3× · see citing works
“(ACE) Milk 28–34 Sun and Jenssen (2012) αs1-CN HIQKEDVPSER Antioxidant Milk 80–90 Baum et al. (2013) αs2-CN TKKTKLTEEEKNRL ACE Milk 148–161 Sistla (2013) β-CN DKIHPF ACE Cheddar, Manchego 47–52 Gómez-Ruiz, Taborda, Amigo, Recio and Ramos (2006) β-CN KVLPVPQ Antihypersensitive Milk 169–175 Park…”
BackgroundAspartic proteinase from Penicillium camemberti: Purification, properties, and substrate specificity
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Self-citationGrowth of Debaryomyces hansenii on a bacterial surface-ripened soft cheese
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Advances in research on calf rennet substitutes and their effects on cheese quality
Liu, X., Wu, Y., Guan, R., Jia, G., Ma, Y., & Zhang, Y. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110704 · Cited by 68 · see citing works
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Alhelli, A. M., Mohammed, N. K., Khalil, E. S., & Hussin, A. S. M. (2021) · AMB Express · doi:10.1186/s13568-021-01205-9 · Cited by 23 · see citing works
Braitmaier, S. H., Wahl, A.-L., Hinrichs, J., & Atamer, Z. (2024) · International Dairy Journal · doi:10.1016/j.idairyj.2024.106056 · Cited by 17 · see citing works
Plant-Based Alternatives to Mold-Ripened Cheeses as an Innovation among Dairy Analogues
Fabiszewska, A. U., Wierzchowska, K., Dębkowska, I., et al. (2024) · Foods · doi:10.3390/foods13142305 · Cited by 17 · see citing works
“Furthermore, the benefits of the presence of LAB and the production of organic acids (e.g., lactic and acetic acids) lead to a lower pH value and enhanced fungal growth [12].”
BackgroundModulating the aroma and taste profile of soybean using novel strains for fermentation
Chin, X. H., Soh, R., Chan, G., Ng, P., Thong, A. Z., Elhalis, H., Kanagasundaram, Y., Chow, Y. Y. S., & Liu, S. (2024) · Current Research in Food Science · doi:10.1016/j.crfs.2024.100933 · Cited by 14 · see citing works
“For example, PC produces proteases that hydrolyse proteins into peptides, which have been shown to increase the umami intensity of Camembert cheese during ripening (Mane and McSweeney, 2020).”
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“The fungi used for cheese making generally exhibit high proteinase and lipolytic activities, although activities vary between strains (Larsen et al., 1998; Larsen and Jensen, 1999; Lessard et al., 2014; Mane and McSweeney, 2020).”
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Biochemical and technological properties of moose (Alces alces) recombinant chymosin
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Enhancing dairy-like aromas and reducing beany flavours in mould-ripened soy cheeses
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“Standard deviations and The high proteolytic activity of molds used in Camembert production results in a cheese with a relatively short ripening period [51]. results of the HSD Tukey test are presented in the Appendix A.”
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JUSTIFICATION OF THE RIPENING PARAMETERS OF CAMAMBER CHEESE PRODUCED USING MODERN DAIRY INGREDIENTS
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“For instance, Aspergillus oryzae produces a milk‑clotting enzyme with a lower Km (2.5x10 ‑2 M), suggesting higher substrate affinity, while Rhizomucor miehei exhibits a markedly lower K m (3x10 ‑3 M), reflecting superior catalytic efficiency in cheese‑making (37,44).”
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The main technological properties of rennet substitutes
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- Authors
- Mane, A., & McSweeney, P. L. H.
- Affiliations
- University College Cork (IE)
- Corresponding author
- McSweeney, Paul L. H.
- Venue
- Journal of Food Biochemistry
- Publisher
- Wiley
- Published
- 2019-11-28
- Volume
- 44
- Issue
- 1
- Pages
- e13101-e13101
- ISSN
- 0145-8884 (ISSN-L)
- 1745-4514
- OpenAlex
- W2989961886
- Cited by
- 35
- References
- 61
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 6 · 2023: 3 · 2022: 5 · 2021: 7 · 2020: 3
- FWCI
- 1.24
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Journal of Food Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Arrow@dit (Dublin Institute of Technology) (submittedVersion)
- Cork Open Research Archive (University College Cork, Ireland) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
- Keywords
- Camembert cheese, farmhouse cheese, cheese ripening, proteolysis, Penicillium camemberti, casein degradation, chymosin, plasmin, cleavage site, cheese peptides, αs1-casein, αs2-casein, β-casein, kappa-casein, proteolytic specificity
- MeSH terms
- Caseins, Cheese, Penicillium, Chymosin, Proteolysis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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