Aspartic Proteases Used in Cheese Making

MEROPS: the peptidase database

Rawlings, N. D., & Barrett, A. J. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.1.325 · Cited by 2,278 · see citing works

The Structure and Function of the Aspartic Proteinases

Davies, D. R. (1990) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.19.060190.001201 · Cited by 658 · see citing works

MEROPS: the peptidase database

Rawlings, N. D. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkh071 · Cited by 378 · see citing works

Structure and function of plant aspartic proteinases

Simões, I., & Faro, C. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04136.x · Cited by 297 · see citing works

Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development

Kageyama, T. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-002-8423-9 · Cited by 256 · see citing works

Microbiology and Biochemistry of Cheese and Fermented Milk

(1997) · Springer eBooks · doi:10.1007/978-1-4613-1121-8 · Cited by 248 · see citing works

Mode of inhibition of acid proteases by pepstatin.

Marciniszyn, J., Hartsuck, J. A., & Tang, J. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32945-9 · Cited by 239 · see citing works

X-ray analyses of aspartic proteinases

Cooper, J. B., Khan, G. N., Taylor, G. L., Tickle, I. J., & Blundell, T. L. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90156-g · Cited by 222 · see citing works

Cheesemaking with vegetable coagulants—the use of <i>Cynara</i> L. for the production of ovine milk cheeses

Roseiro, L. B., Barbosa, M., Ames, J. M., & Wilbey, R. A. (2003) · International Journal of Dairy Technology · doi:10.1046/j.1471-0307.2003.00080.x · Cited by 200 · see citing works

Commercial Levels of Chymosin Production by Aspergillus

Dunn-Coleman, N. S., Bloebaum, P., Berka, R. M., Bodie, E. A., Robinson, N. A., Armstrong, G., Ward, M. P., Przetak, M. M., Carter, G. L., LaCost, R., et al. (1991) · Nature Biotechnology · doi:10.1038/nbt1091-976 · Cited by 167 · see citing works

Mozzarella Cheese: Impact of Cooking Temperature on Chemical Composition, Proteolysis and Functional Properties

Yun, J. J., Kiely, L. J., Barbano, D. M., & Kindstedt, P. S. (1993) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(93)77708-5 · Cited by 139 · see citing works

Flap Position of Free Memapsin 2 (β-Secretase), a Model for Flap Opening in Aspartic Protease Catalysis ,

Hong, L., & Tang, J. (2004) · Biochemistry · doi:10.1021/bi0498252 · Cited by 135 · see citing works

The three‐dimensional structure of recombinant bovine chymosin at 2.3 Å resolution

Gilliland, G. L., Winborne, E., Nachman, J., & Wlodawer, A. (1990) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340080110 · Cited by 118 · see citing works

X-ray analyses of aspartic proteinases

Blundell, T. L., Jenkins, J. A., Sewell, B. T., Pearl, L. H., Cooper, J. B., Tickle, I. J., Veerapandian, B., & Wood, S. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90084-y · Cited by 115 · see citing works

The complete amino acid sequence of prochymosin.

Foltmann, B., Pedersen, V. B., Jacobsen, H., Kauffman, D. L., & Wybrandt, G. B. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.6.2321 · Cited by 109 · see citing works

Investigations on the Activation of Bovine Prochymosin

Pedersen, V. B., Christensen, K. A., & Foltmann, B. (1979) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1979.tb12927.x · Cited by 102 · see citing works

Analysis of crystal structures of aspartic proteinases: On the role of amino acid residues adjacent to the catalytic site of pepsin‐like enzymes

Andreeva, N. S., & Rumsh, L. D. (2001) · Protein Science · doi:10.1110/ps.25801 · Cited by 96 · see citing works

Rennets: their role in milk coagulation and cheese ripening

Fox, P. F., & McSweeney, P. L. H. (1997) · Springer eBooks · doi:10.1007/978-1-4613-1121-8_1 · Cited by 96 · see citing works

Crystal Structure of Cardosin A, a Glycosylated and Arg-Gly-Asp-containing Aspartic Proteinase from the Flowers ofCynara cardunculus L.

Frazão, C., Bento, I., Costa, J., Soares, C. M., Verı́ssimo, P., Faro, C., Pires, E., Cooper, J. B., & Carrondo, M. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27694 · Cited by 93 · see citing works

Chymosin and aspartic proteinases

Chitpinityol, S., & Crabbe, M. J. C. (1998) · Food Chemistry · doi:10.1016/s0308-8146(97)00090-3 · Cited by 92 · see citing works

X-ray analyses of aspartic proteinases IV

Newman, M., Safro, M. G., Frazão, C., Khan, G. N., Zdanov, A. S., Tickle, I. J., Blundell, T. L., & Andreeva, N. S. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90934-x · Cited by 90 · see citing works

Cardosin A, an abundant aspartic proteinase, accumulates in protein storage vacuoles in the stigmatic papillae of Cynara cardunculus L.

Ramalho-Santos, M., Pissarra, J., Veríssimo, P., Pereira, S., Salema, R., Pires, E., & Faro, C. J. (1997) · Planta · doi:10.1007/s004250050183 · Cited by 88 · see citing works

Identification and proteolytic processing of procardosin A

Ramalho‐Santos, M., Verı́ssimo, P., Cortes, L., Samyn, B., BEEUMEN, J. V., Pires, E., & Faro, C. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2550133.x · Cited by 81 · see citing works

Analysis of crystal structures of aspartic proteinases: On the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes

Andreeva, N. S. (2001) · Protein Science · doi:10.1110/ps.ps.25801 · Cited by 78 · see citing works

Cloning and sequencing of a gene for Mucor rennin, an aspartate protease fromMucor pusillus

Tonouchi, N., Shoun, H., Uozumi, T., & Beppu, T. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.19.7557 · Cited by 75 · see citing works

Molecular cloning and characterization of cDNA encoding cardosin B, an aspartic proteinase accumulating extracellularly in the transmitting tissue of Cynara cardunculus L.

Vieira, M., Pissarra, J., Verı́ssimo, P., Castanheira, P., Costa, Y., Pires, E., & Faro, C. (2001) · Plant Molecular Biology · doi:10.1023/a:1010675015318 · Cited by 74 · see citing works

Purification of cynarases from artichoke (Cynara scolymus L.): enzymatic properties of cynarase A

Sidrach, L., García-Cánovas, F., Tudela, J., & Neptuno Rodríguez-López, J. (2005) · Phytochemistry · doi:10.1016/j.phytochem.2004.10.005 · Cited by 74 · cited 1× · see citing works

The primary structure of calf chymosin.

Foltmann, B., Pedersen, V. B., Kauffman, D. L., & Wybrandt, G. B. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86912-0 · Cited by 74 · see citing works

Chymosin: A short review on foetal and neonatal gastric proteases

Foltmann, B. (1992) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.1080/00365519209104656 · Cited by 73 · see citing works

The Saposin-like Domain of the Plant Aspartic Proteinase Precursor Is a Potent Inducer of Vesicle Leakage

Egas, C., Lavoura, N., Resende, R., Brito, R. M. M., Pires, E., de Lima, M. C. P., & Faro, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006093200 · Cited by 71 · see citing works

Effects of glycosylation on the secretion and enzyme activity of Mucor rennin, an aspartic proteinase of Mucor pusillus, produced by recombinant yeast.

Aikawa, J.-I., Yamashita, T., Nishiyama, M., Horinouchi, S., & Beppu, T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77441-3 · Cited by 65 · see citing works

Bovine chymosin

Mohanty, A. K., Mukhopadhyay, U. K., Grover, S., & Batish, V. K. (1999) · Biotechnology Advances · doi:10.1016/s0734-9750(99)00010-5 · Cited by 64 · see citing works

Purification, cloning and autoproteolytic processing of an aspartic proteinase from <i>Centaurea calcitrapa</i>

Domingos, A., Cardoso, P. C., Xue, Z., Clemente, A., Brodelius, P. E., & Pais, M. S. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2000.01780.x · Cited by 64 · cited 1× · see citing works

Processing, Activity, and Inhibition of Recombinant Cyprosin, an Aspartic Proteinase from Cardoon (Cynara cardunculus)

White, P. C., Cordeiro, M. C., Arnold, D., Brodelius, P. E., & Kay, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.16685 · Cited by 60 · see citing works

Recombinant Lamb Chymosin as an Alternative Coagulating Enzyme in Cheese Production

Rogelj, I., Perko, B., Francky, A., Penca, V., & Pungerčar, J. (2001) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(01)74561-4 · Cited by 59 · see citing works

Mozzarella Cheese: Impact of Coagulant Type on Functional Properties

Yun, J. J., Kiely, L. J., Kindstedt, P. S., & Barbano, D. M. (1993) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(93)77707-3 · Cited by 56 · see citing works

X-ray Analyses of Aspartic Proteinases

Newman, M., Watson, F. E., Roychowdhury, P., Jones, H., Badasso, M. O., Cleasby, A., Wood, S., Tickle, I. J., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1141 · Cited by 50 · see citing works

X-ray analyses of aspartic proteinases. V. Structure and refinement at 2.0 A resolution of the aspartic proteinase from Mucor pusillus.

Newman, M., Watson, F. E., Roychowdhury, P., et al. (1993) · PubMed · Cited by 46 · see citing works

Activation, Proteolytic Processing, and Peptide Specificity of Recombinant Cardosin A

Castanheira, P., Samyn, B., Sergeant, K., Clemente, J. C., Dunn, B. M., Pires, E., BEEUMEN, J. V., & Faro, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412076200 · Cited by 44 · see citing works

Secretion by yeast of the zymogen form of Mucor rennin, an aspartic proteinase of Mucor pusillus, and its conversion to the mature form

Hiramatsu, R., Aikawa, J.-I., Horinouchi, S., & Beppu, T. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84786-5 · Cited by 42 · see citing works

Five Atomic Resolution Structures of Endothiapepsin Inhibitor Complexes: Implications for the Aspartic Proteinase Mechanism

Coates, L., Erskine, P. T., Crump, M. P., Wood, S., & Cooper, J. B. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00197-3 · Cited by 42 · see citing works

Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15 Å resolution 1 1Edited by R. Huber

Yang, J. P., Teplyakov, A., & Quail, J. W. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0968 · Cited by 42 · see citing works

Isolation, purification and characterization of chymosin from riverine buffalo (Bubalos bubalis)

Mohanty, A. K., Mukhopadhyay, U. K., Kaushik, J. K., Grover, S., & Batish, V. K. (2003) · Journal of Dairy Research · doi:10.1017/s0022029902005927 · Cited by 41 · see citing works

Molecular cloning and expression in yeast of caprine prochymosin

Vega-Hernández, M. C., Gómez-Coello, A., Villar, J. M., & Claveríe‐Martín, F. (2004) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2004.06.002 · Cited by 39 · see citing works

Combined Use of Chymosin and Protease from Cryphonectria parasitica for Control of Meltability and Firmness of Cheddar Cheese

Kim, S.-Y., Gunasekaran, S., & OLSON, N. F. (2004) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(04)73166-5 · Cited by 39 · see citing works

The three-dimensional structure at 2.4 Å resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae

Aguilar, C. F., Cronin, N., Badasso, M. O., Dreyer, T., Newman, M., Cooper, J. B., Hoover, D. J., Wood, S., Johnson, M. S., & Blundell, T. L. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0880 · Cited by 38 · see citing works

Post X‐ray crystallographic studies of chymosin: the existence of two structural forms and the regulation of activity by the interaction with the histidine‐proline cluster of κ‐casein

Gustchina, E., Rumsh, L. D., Ginodman, L. M., Majer, P., & Andreeva, N. S. (1996) · FEBS Letters · doi:10.1016/0014-5793(95)01488-8 · Cited by 32 · see citing works

Crystal Structure of Aspartic Proteinase from Irpex lacteus in Complex with Inhibitor Pepstatin

Fujimoto, Z., Fujii, Y., Kaneko, S., Kobayashi, H., & Mizuno, H. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.06.049 · Cited by 32 · see citing works

Catalytic pathway of aspartic peptidases

James, M. N. G. (2004) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-079611-3.50010-0 · Cited by 25 · see citing works

A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure

Groves, M. R., Dhanaraj, V., Badasso, M. O., Nugent, P., Pitts, J. E., Hoover, D. J., & Blundell, T. L. (1998) · Protein Engineering Design and Selection · doi:10.1093/protein/11.10.833 · Cited by 25 · see citing works

Involvement of a residue at position 75 in the catalytic mechanism of a fungal aspartic proteinase, Rhizomucor pusilus pepsin. Replacement of tyrosine 75 on the flap by asparagine enhances catalytic efficiency

Park, Y.-N., Aikawa, J.-I., Nishiyama, M., Horinouchi, S., & Beppu, T. (1996) · Protein Engineering Design and Selection · doi:10.1093/protein/9.10.869 · Cited by 25 · see citing works

Chymosin: A short review on foetal and neonatal gastric proteases

Foltmann, B. (1992) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365519209104656 · Cited by 24 · see citing works

Cardosin A and B, Aspartic Proteases from the Flowers of Cardoon

Faro, C., Verı́ssimo, P., Lin, Y., Tang, J., & Pires, E. (1995) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-1871-6_49 · Cited by 20 · see citing works

The primary structure and enzymic properties of porcine prochymosin and chymosin

Houen, G., Madsen, M. T., Harlow, K. W., Lønblad, P. B., & Foltmann, B. (1996) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/1357-2725(96)00002-7 · Cited by 20 · see citing works

Complete primary structure of lamb preprochymosin deduced from cDNA

Pungerčar, J., Štrukelj, B., Gubenšek, F., Türk, V., & Kregar, I. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.15.4602 · Cited by 18 · see citing works

Mutation of a fungal aspartic proteinase, Mucor pusillus rennin, to decrease thermostability for use as a milk coagulant

Yamashita, T., Higashi, S., Higashi, T., Machida, H., Iwasaki, S., Nishiyama, M., & Beppu, T. (1994) · Journal of Biotechnology · doi:10.1016/0168-1656(94)90116-3 · Cited by 16 · see citing works

Structure of theRhizomucor mieheiaspartic proteinase complexed with the inhibitor pepstatin A at 2.7 Å resolution

Yang, J. P., & Quail, J. W. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998013961 · Cited by 15 · see citing works

Proteolytic Activities of Suparen and Rennilase on Buffalo, Cow, and Goat Whole Casein and β-Casein

Awad, S., Qiaoqian, P. E. N. G., & Puhan, Z. (1999) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf981365u · Cited by 14 · see citing works

Physicochemical, molecular and immunological characterization of camel calf rennet: a comparison with buffalo rennet

El‐Agamy, E. I. (2000) · Journal of Dairy Research · doi:10.1017/s0022029999003957 · Cited by 14 · see citing works

Milk-clotting enzyme from Irpex lacteus as a calf rennet substitute for cheddar cheese manufacture.

Kobayashi, H., Kusakabe, I., & Murakami, K. (1985) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.49.1605 · Cited by 13 · see citing works

A basic residue at position 36p of the propeptide is not essential for the correct folding and subsequent autocatalytic activation of prochymosin

Francky, A., Mozetič-Francky, B., Štrukelj, B., Gruden, K., Ritonja, A., Križaj, I., Kregar, I., Pain, R. H., & Pungerčar, J. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02119.x · Cited by 12 · see citing works

Pepsin A

Tang, J. (2004) · Handbook of Proteolytic Enzymes · doi:10.1016/b978-0-12-079611-3.50011-2 · Cited by 11 · see citing works

Replacements of Amino Acid Residues at Subsites and Their Effects on the Catalytic Properties of Rhizomucor pusillus Pepsin, an Aspartic Proteinase from Rhizomucor pusillus

Aikawa, J.-I., Park, Y.-N., Sugiyama, M., Nishiyama, M., Horinouchi, S., & Beppu, T. (2001) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a002921 · Cited by 9 · see citing works

Structural and functional determinants of Mucor miehei protease

Rickert, W. S., & McBride-Warren, P. A. (1974) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(74)90033-6 · Cited by 7 · see citing works

Crystallization and preliminary X-ray structure solution ofRhizomucor mieheiaspartic proteinase

Jia, Z., Vandonselaar, M., Schneider, P., & Quail, J. W. (1995) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744499401156x · Cited by 5 · see citing works

Impact of microbial proteases on biotechnological industries

Banerjee, G., & Ray, A. K. (2017) · Biotechnology and Genetic Engineering Reviews · doi:10.1080/02648725.2017.1408256 · Cited by 109 · see citing works

Protease and lipase activities of fungal and bacterial strains derived from an artisanal raw ewe's milk cheese

Ozturkoglu‐Budak, S., Wiebenga, A., Bron, P. A., & de Vries, R. P. (2016) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2016.08.007 · Cited by 105 · see citing works

Microbial aspartic proteases: current and potential applications in industry

Theron, L. W., & Divol, B. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-6035-6 · Cited by 104 · see citing works

Plant Milk-Clotting Enzymes for Cheesemaking

Nicosia, F. D., Puglisi, I., Pino, A., Caggia, C., & Randazzo, C. L. (2022) · Foods · doi:10.3390/foods11060871 · Cited by 95 · see citing works

Aspartic proteinases from Mucor spp. in cheese manufacturing

Yeğin, S., Fernández‐Lahore, M., Salgado, A. J. G., Güvenç, U., Göksungur, Y., & Tarı, C. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-3020-6 · Cited by 93 · see citing works

Importance of enzyme specificity and stability for the application of proteases in greener industrial processing- a review

Sujitha, P., & Shanthi, C. (2023) · Journal of Cleaner Production · doi:10.1016/j.jclepro.2023.138915 · Cited by 68 · see citing works

Progress in the field of aspartic proteinases in cheese manufacturing: structures, functions, catalytic mechanism, inhibition, and engineering

Yeğin, S., & Dekker, P. (2013) · Dairy Science and Technology · doi:10.1007/s13594-013-0137-2 · Cited by 68 · see citing works

One-step recovery of latex papain from Carica papaya using three phase partitioning and its use as milk-clotting and meat-tenderizing agent

Hafid, K., John, J., Sayah, T. M., Domínguez, R., Becila, S., Lamri, M., Dib, A. L., Lorenzo, J. M., & Gagaoua, M. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.10.048 · Cited by 65 · see citing works

Comparison of the Hydrolysis of Bovine κ-Casein by Camel and Bovine Chymosin: A Kinetic and Specificity Study

Møller, K. K., Rattray, F. P., Sørensen, J. C., & Ardö, Y. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf300557d · Cited by 45 · see citing works

The Texture of Camel Milk Cheese: Effects of Milk Composition, Coagulants, and Processing Conditions

Mbye, M., Ayyash, M. M., Abu‐Jdayil, B., & Kamal‐Eldin, A. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.868320 · Cited by 35 · see citing works

Marine enzymes and food industry: insight on existing and potential interactions

Fernandes, P. C. D. B. (2014) · Frontiers in Marine Science · doi:10.3389/fmars.2014.00046 · Cited by 34 · see citing works

Enzymatic extract from flowers of Algerian spontaneous Cynara cardunculus: Milk‐clotting properties and use in the manufacture of a Camembert‐type cheese

Zikiou, A., & Zidoune, M. N. (2018) · International Journal of Dairy Technology · doi:10.1111/1471-0307.12563 · Cited by 31 · see citing works

Thermostable trypsin‐like protease by Penicillium roqueforti secreted in cocoa shell fermentation: Production optimization, characterization, and application in milk clotting

Nogueira, L. S., Tavares, I. M. D. C., Santana, N. B., Ferrão, S. P. B., Teixeira, J. M., Costa, F. S., Silva, T. P., Pereira, H. J. V., Irfan, M. I., Bilal, M., et al. (2021) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2268 · Cited by 25 · see citing works

Molecular modification and biotechnological applications of microbial aspartic proteases

Herman, R. A., Ayepa, E., Zhang, W.-X., Li, Z.-N., Zhu, X., Ackah, M., Yuan, S.-S., You, S., & Wang, J. (2024) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2023.2171850 · Cited by 20 · see citing works

PEMBUATAN DAN KARAKTERISASI HIDROLISAT PROTEIN DARI IKAN LELE DUMBO (Clarias gariepinus) MENGGUNAKAN ENZIM PAPAIN Production and Characterization of Protein Hydrolysates from African Catfish (Clarias gariepinus) using Papain

Salamah, E., Nurhayati, ‪., Widadi, I. R., & Widadi (2012) · Jurnal Pengolahan Hasil Perikanan Indonesia · doi:10.17844/jphpi.v15i1.5328 · Cited by 20 · see citing works

Extracellular peptidases from Deinococcus radiodurans

Dalmaso, G. Z. L., Lage, C. A. S., Mazotto, A. M., Dias, E. P. D. S., Caldas, L. A., Ferreira, D. F., & Vermelho, A. B. (2015) · Extremophiles · doi:10.1007/s00792-015-0773-y · Cited by 19 · see citing works

A Thermolabile Aspartic Proteinase from Mucor mucedo DSM 809: Gene Identification, Cloning, and Functional Expression in Pichia pastoris

Yeğin, S., & Fernández‐Lahore, M. (2012) · Molecular Biotechnology · doi:10.1007/s12033-012-9608-6 · Cited by 19 · see citing works

Cloning and expression of an active aspartic proteinase from Mucor circinelloides in Pichia pastoris

Salgado, J. A. G., Kangwa, M., & Fernández‐Lahore, M. (2013) · BMC Microbiology · doi:10.1186/1471-2180-13-250 · Cited by 18 · see citing works

Quality evaluation of mozzarella cheese made from buffalo milk by using paneer booti (Withania coagulans) and calf rennet

Nawaz, M. A., Masud, T., & Sammi, S. (2011) · International Journal of Dairy Technology · doi:10.1111/j.1471-0307.2010.00653.x · Cited by 18 · see citing works

Aspartic Proteases in Food Industry

Nair, I. C., & Jayachandran, K. (2018) · Energy, environment, and sustainability · doi:10.1007/978-981-13-3263-0_3 · Cited by 14 · see citing works

Effect of different storage conditions on coagulating properties and cheese quality of Withania coagulans extract

Qazalbash, M. A., Masud, T., Sammi, S., Khan, R. S., & Latif, A. (2017) · International Journal of Dairy Technology · doi:10.1111/1471-0307.12481 · Cited by 10 · see citing works

Role of Microbial Cultures and Enzymes During Cheese Production and Ripening

Ozturkoglu‐Budak, S., Koçak, C., Bron, P. A., & de Vries, R. P. (2018) · Advances in medical technologies and clinical practice book series · doi:10.4018/978-1-5225-5363-2.ch010 · Cited by 7 · see citing works

Microbial proteases—robust biocatalytic tools for greener biotechnology

Akram, Z., Asgher, M., & Qamar, S. A. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-99476-7.00004-1 · Cited by 5 · see citing works

Comprehensive bioinformatics-based annotation and functional characterization of bovine chymosin protein revealed novel biological insights

Amjad, H., Saleem, F., Ahmad, M., Nisar, U., & Dar, H. A. (2023) · Food Chemistry Molecular Sciences · doi:10.1016/j.fochms.2023.100191 · Cited by 4 · see citing works

Innovative Approach of Cheese Making from Camel Milk: A Review

Bekele, B. (2023) · Food science and nutrition · doi:10.5772/intechopen.108700 · Cited by 3 · see citing works

Recent trends in biocatalysis and its application in the food industry

Borges, S., Brassesco, M. E., Cunha, S. A., Coscueta, E. R., & Pintado, M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95996-4.00016-2 · Cited by 2 · see citing works

Estudios de Caracterización Cinética y Fisicoquímica de una Proteinasa Aspártica Aislada de Frutos Maduros de Salpichroa origanifolia

Rocha, G. E., Fernández, G., & Parisi, M. G. (2010) · Información tecnológica · doi:10.4067/s0718-07642010000200004 · Cited by 2 · see citing works

Structural and functional peculiarities of aspartic proteases of basidiomycetes

Sakovich, V. V. (2020) · Biopolymers and Cell · doi:10.7124/bc.000a2a · Cited by 1 · see citing works

Proteases: an unexplored enzyme for biomass conversion

Srivastava, N., Mishra, P. K., & Upadhyay, S. N. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-821010-9.00008-5 · Cited by 1 · see citing works

PENINGKATAN DAYA SAING DAN NILAI TAMBAH SUSU KERBAU PERAH MELALUI PENGOLAHAN MENJADI KEJU YANG DIPERKAYA DENGAN ASAM LINOLEAT

Dha, E. D. (2011)

Production of Milk Clotting Aspartic Protease from Bacterial Species Isolated from Dumping Site of Mehmood Booti, Lahore

Ghafoor, K., & Majeed, T. (2022) · MARKHOR (The Journal of Zoology) · doi:10.54393/mjz.v3i1.46

Influence of different milk-clotting enzymes on the quality and shelf life of semihard cheeses

Сергеевич, М. Д., Абрамов, Д. В., Delitskaya, I. N., & Bukcharina, G. B. (2024) · Food systems · doi:10.21323/2618-9771-2023-6-4-477-487

Development of a plant-based milk-clotting enzyme and a debittering microbial culture for the formulation of halal-certified healthy cheese

Nicosia, F. D. (2024) · doi:10.47328/ufvbbt.2024.152

Plant-sourced proteases used in cheese making.

Uzkuç, H., & Yüceer, Y. K. (2017) · Çanakkale Onsekiz Mart University AVESIS

Proteolysis in Cheese during Ripening

Fox, P. F., Singh, T. K., & McSweeney, P. L. H. (2005) · Elsevier eBooks · doi:10.1533/9780857093066.1 · Cited by 47 · see citing works

Progress in the field of aspartic proteinases in cheese manufacturing: structures, functions, catalytic mechanism, inhibition, and engineering

Yeğin, S., & Dekker, P. (2013) · Dairy Science and Technology · doi:10.1007/s13594-013-0137-2 · Cited by 68 · see citing works

Rapid preliminary test of microbial proteases for applicability in cheese-making.

Vámos, L., Pozsar, K., & Szekeres, A. (1970) · Microbiologia

Immobilization of some proteases for cheese manufacture

Prasad, Y. S., & Mathur, M. P. (2014)