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AFPLEFEREL + H2O
AFPLEF + EREL
modified peptide substrate based on residues 165-174 of proopiomelanocortin
-
-
?
AFPLEFFREL + H2O
AFPLEF + FREL
modified peptide substrate based on residues 165-174 of proopiomelanocortin
-
-
?
AFPLEFIREL + H2O
AFPLEF + IREL
modified peptide substrate based on residues 165-174 of proopiomelanocortin
-
-
?
AFPLEFKREL + H2O
AFPLEF + KREL
modified peptide substrate based on residues 165-174 of proopiomelanocortin
-
-
?
Abz-A-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
Abz-A-A-F-F-A-A-p-nitroanilide + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
Abz-A-A-F-F-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
Abz-A-A-F-F-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
Abz-A-A-F-F-pnA + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
Abz-A-F-F-A-A-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
?
-
low molecular weight, fluorogenic peptide substrate
-
-
?
acid denatured hemoglobin + H2O
?
-
-
-
-
?
alphaS-casein + H2O
?
-
-
-
-
?
alphas1-casein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
beta-chain of proteolytic insulin + H2O
?
-
general proteolytic activity
-
-
?
bovine kappa-casein + H2O
?
bovine kappa-casein + H2O
para-kappa-casein + caseinomacropeptide
-
the enzyme cleaves the Phe105-Met106 bond of kappa-casein
-
-
?
bovine kappa-casein residues 97-112 + H2O
?
-
substrate binds in an extended conformation with charged residues on either side of the scissile bond playing an important role in stabilizing the binding pose. Substrate residues Lys111 and Lys112 bind to the N-terminal domain of chymosin displacing a conserved water molecule. A cluster of histidine and proline residues, His98-Pro99-His100-Pro101-His102, in kappa-casein binds to the C-terminal domain of the protein, where neighboring conserved arginine residue Arg97 is important for stabilizing the binding pose. The catalytic site including the catalytic water molecule is stable in the starting conformation of the general acid/base catalytic mechanism for 18 ns of molecular dynamics simulations
-
-
?
His-Pro-His-Pro-His-Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O
His-Pro-His-Pro-His-Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
His-Pro-His-Pro-His-Leu-Ser-Phe-Phe(NO2)-Ala-Ile-Pro-Pro-Lys-Lys + H2O
?
-
-
-
-
?
HPHPHLSFMAIPPKK + H2O
?
-
-
-
-
?
kappa-casein + H2O
casein macropeptide + para-kappa-casein
kappa-casein + H2O
caseinmacropeptide + para-kappa-casein
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
kappa-casein + H2O
para-kappa-casein + macropeptide
-
kappa-casein is the primary substrate for the chymosin action
-
-
?
L-leucine-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-S-F-M-A-I-P-NH2 + H2O
?
-
hepapeptide, a fragment of the native chymosin substrate kappa-casein, is most efficiently cleaved by native calf chymosin and less efficiently by transgenic chymosin and recombinant chymosin
-
-
?
Leu-Ser-Phe(NO2)-Nle-Ala-Leu-OMe + H2O
?
-
-
-
-
?
Leu-Ser-Phe-Met-Ala-Ile-O-methyl ester + H2O
Leu-Ser-Phe + Met-Ala-Ile-O-methyl ester
-
part of the bovine kappa-casein sequence
-
?
Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O
Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
Leu-Ser-Phe-Met-Ala-O-methyl ester + H2O
Leu-Ser-Phe + Met-Ala-O-methyl ester
-
part of the bovine kappa-casein sequence
-
?
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu-OH + H2O
Lys-Pro-Ala-Glu-Phe + Phe(NO2)-Ala-Leu
Lys-Pro-Leu-Glu-Phe-Phe(NO2)-Arg-Leu + H2O
Lys-Pro-Leu-Glu-Phe + Phe(NO2)-Arg-Leu
-
-
-
?
o-aminobenzoyl-Ala-Ala-Phe-Phe-Ala-Ala-NH-C6H4NO2 + H2O
o-aminobenzoyl-Ala-Ala-Phe + Phe-Ala-Ala-NHC6H4NO2
-
-
-
?
o-aminobenzoyl-Ala-Ala-Phe-Phe-NH-C6H4-NO2 + H2O
o-aminobenzoyl-Ala-Ala-Phe + Phe-NH-C6H4-NO2
-
-
-
?
Pro-His-Leu-Ser-Phe-Met-Ala-Ile-O-methyl ester + H2O
Pro-His-Leu-Ser-Phe + Met-Ala-Ile-O-methyl ester
-
part of the bovine kappa-casein sequence
-
?
Ser-Phe-Met-Ala-Ile-O-methyl ester + H2O
Ser-Phe + Met-Ala-Ile-O-methyl ester
-
part of the bovine kappa-casein sequence
-
?
skim milk + H2O
?
-
-
-
-
?
skimmed milk + H2O
?
-
-
-
-
?
undecapeptide analogue to chymosin sensitive region of bovine kappa casein
?
-
synthetic substrate
-
-
?
undecapeptide analogue to chymosin sensitive region of camel kappa casein
?
-
synthetic substrate
-
-
?
whole milk + H2O
?
-
-
-
-
?
YGISSKFCE + H2O
YGISSKF + L-Cys-L-Glu
-
modified peptide based on prochymosin sequence
100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFfE + H2O
YGISSKF + FE
-
modified peptide based on prochymosin sequence
100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFHE + H2O
YGISSKF + His-Glu
-
modified peptide based on prochymosin sequence
51% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFIE + H2O
YGISSKF + Ile-Glu
-
modified peptide based on prochymosin sequence
54% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFKE + H2O
YGISSKF + Lys-Glu
-
modified peptide based on prochymosin sequence
33% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFLE + H2O
YGISSKF + L-Leu-L-Glu
-
modified peptide based on prochymosin sequence
42% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFME + H2O
YGISSKF + L-Met-L-Glu
-
modified peptide based on prochymosin sequence
52% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFNE + H2O
YGISSKF + L-Asn-L-Glu
-
modified peptide based on prochymosin sequence
33% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFRE + H2O
YGISSKF + Arg-Glu
-
modified peptide based on prochymosin sequence
59% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFVE + H2O
YGISSKF + Val-Glu
-
modified peptide based on prochymosin sequence
36% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFWE + H2O
YGISSKF + Trp-Glu
-
modified peptide based on prochymosin sequence
100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
YGISSKFYE + H2O
YGISSKF + L-Tyr-L-Glu
-
modified peptide based on prochymosin sequence
100% cleavage at enzyme to substrate ratio of 1:1, pH 6.2, 16 h
-
?
additional information
?
-
kappa-casein + H2O
?
-
-
-
?
kappa-casein + H2O
?
-
-
-
-
?
kappa-casein + H2O
?
-
-
-
?
kappa-casein + H2O
?
the enzyme cleaves the Phe105-Met106 bond of kappa-casein, releasing its predominantly negatively charged C-terminus
-
-
?
alpha-casein + H2O
?
-
-
-
-
?
alpha-casein + H2O
?
-
at 50% casein degradation, 15% more of alphaS1-casein with eight phosphate groups is hydrolysed compared with alphaS1-casein with nine phosphate groups in chymosin-induced milk gels
-
-
?
beta-casein + H2O
?
-
-
-
-
?
beta-casein + H2O
?
-
occurs during the long period of renneting
-
-
?
beta-casein + H2O
?
-
in sodium caseinate solutions, more than 10% more beta-casein A2 is degraded compared with beta-casein A1 and B at 50% casein degradation
-
-
?
bovine kappa-casein + H2O
?
-
-
-
-
?
bovine kappa-casein + H2O
?
-
kappa-casein samples are a mixture of monomers and aggregates at room temperature and pH 7.2, and that heating produces extensive kappa-casein aggregation.The initial polymerization or association state of kappa-casein affects on the aggregation stage after the enzymatic action of chymosin. Sucrose and lactose also affect the aggregation of proteolized particles of kappa-chymosin
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
the enzyme breaks the bond between Phe-105 and Met-106 in the casein and initiates the coagulation of milk
-
-
?
His-Pro-His-Pro-His-Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O
His-Pro-His-Pro-His-Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
-
part of the bovine kappa-casein sequence
-
?
His-Pro-His-Pro-His-Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O
His-Pro-His-Pro-His-Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
-
part of the bovine kappa-casein sequence
-
?
kappa-casein + H2O
?
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
36869, 36870, 36871, 36872, 36873, 36874, 36875, 36876, 36878, 36879, 36880, 36882, 36883, 36889, 36890, 36893, 36894 -
-
?
kappa-casein + H2O
?
-
cleaves a single bond between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
?
-
involved in milk clotting
-
-
?
kappa-casein + H2O
?
-
the enzyme cleaves the Phe105-Met106 bond
-
-
?
kappa-casein + H2O
?
-
the bond Phe105-Met106 is the main hydrolyzed bond by the enzyme
-
-
?
kappa-casein + H2O
casein macropeptide + para-kappa-casein
-
-
-
-
?
kappa-casein + H2O
casein macropeptide + para-kappa-casein
-
cleaves a single bond between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
caseinmacropeptide + para-kappa-casein
-
-
-
-
?
kappa-casein + H2O
caseinmacropeptide + para-kappa-casein
-
cleaves a single bond between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
-
-
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction
?
kappa-casein + H2O
p-kappa-casein + glycomacropeptide
-
cleaves a single bond in kappa-casein between phenylalanine 105 and methionine 106
p-kappa-casein i.e. N-terminal fraction, glycomacropeptide i.e. C-terminal fraction
?
Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O
Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
-
part of the bovine kappa-casein sequence
-
?
Leu-Ser-Phe-Met-Ala-Ile-Pro-NH2 + H2O
Leu-Ser-Phe + Met-Ala-Ile-Pro + NH3
-
part of the bovine kappa-casein sequence
-
?
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu-OH + H2O
Lys-Pro-Ala-Glu-Phe + Phe(NO2)-Ala-Leu
-
-
-
?
Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu-OH + H2O
Lys-Pro-Ala-Glu-Phe + Phe(NO2)-Ala-Leu
-
-
-
?
milk + H2O
?
-
-
-
-
?
milk + H2O
?
-
the maximum increase on milk-clotting activity is 10% for recombinant chymosin at 212MPa/5 min/10°C
-
-
?
additional information
?
-
bovine chymosin is a poor coagulant for camel milk
-
-
?
additional information
?
-
-
bovine chymosin is a poor coagulant for camel milk
-
-
?
additional information
?
-
-
the enzyme has milk coagulation bioactivity
-
-
?
additional information
?
-
-
in the process of milk coagulation under the action of chymosin, alpha- and beta-caseins are not hydrolyzed
-
-
?
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Malak, C.A.A.; El Adab, I.F.G.A.; Vukashinovic, V.; Zalunin, I.A.; Timokhina, E.A.; Lavrenova, G.I.; Stepanov, V.M.
Buffalo (Bos buffali L.) chymosin purification and properties
Comp. Biochem. Physiol. B
113
57-62
1996
Bos taurus
brenda
Moir, D.; Mao, J.I.; Schumm, J.W.; Vovis, G.F.; Alford, B.L.; Taunton-Rigby, A.
Molecular cloning and characterization of double-stranded cDNA coding for bovine chymosin
Gene
19
127-138
1982
Bos taurus
brenda
Beppu, T.
The cloning and expression of chymosin (rennin) genes in microorganisms
Trends Biotechnol.
1
85-89
1983
Bos taurus
-
brenda
Gustchina, E.; Rumsh, L.; Ginodman, L.; Majer, P.; Andreeva, N.
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 kappa-casein
FEBS Lett.
379
60-62
1996
Bos taurus
brenda
Kleinert, T.; Lange, I.; Roesicke, B.; Honig, A.; Schleusener, R.
Characterization and preparation of chymosin from calf rennet samples by means of isoelectric focusing
Acta Biotechnol.
8
367-375
1988
Bos taurus
-
brenda
Zayas, J.F.
Properties and quality characteristics of rennin extracted by ultrasound
Biotechnol. Bioeng.
29
969-975
1987
Bos taurus
brenda
Kawaguchi, Y.; Kosugi, S.; Sasaki, K.; Uozumi, T.; Beppu, T.
Production of chymosin in Escherichia coli cells and its enzymatic properties
Agric. Biol. Chem.
51
1871-1877
1987
Bos taurus
-
brenda
McCaman, M.T.; Andrews, W.H.; Files, J.G.
Enzymatic properties and processing of bovine prochymosin synthezised in Escherichia coli
J. Biotechnol.
2
177-190
1985
Bos taurus
-
brenda
Raap, J.; Kerling, K.E.T.; Vreeman, H.J.; Visser, S.
Peptide substrates for chymosin (rennin): conformational studies of kappa-casein and some kappa-casein-related oligopeptides by circular dichroism and secondary structure prediction
Arch. Biochem. Biophys.
221
117-124
1983
Bos taurus
brenda
Miyoshi, M.; Yoon, C.H.; Ibuki, F.; Kanamori, M.
The characterization of rennin action on kappa-casein using CM-cellulose
Agric. Biol. Chem.
40
347-352
1976
Bos taurus
-
brenda
Chang, W.J.; Takahashi, K.
The structure and function of acid proteases. III. Isolation and characterization of the active-site peptides from bovine rennin
J. Biochem.
76
467-474
1974
Bos taurus
brenda
Williams, M.G.; Wilsher, J.; Nugent, P.; Mills, A.; Dhanaraj, V.; Fabry, M.; Sedlacek, J.; Uusitalo, J.M.; Penttila, M.E.; Pitts, J.E.; Blundell, T.L.
Mutagenesis, biochemical characterization and X-ray structural analysis of point mutants of bovine chymosin
Protein Eng.
10
991-997
1997
Bos taurus
brenda
Foltmann, B.
Prochymosin and chymosin (prorennin and rennin)
Methods Enzymol.
19
421-436
1970
Bos taurus
-
brenda
Azuma, N.; Kaminogawa, S.; Yamauchi, K.
Properties of glycomacropeptide and para-kappa-casein derived from human kappa-casein and comparison of human and bovine kappa-casein as to susceptibility to chymosin and pepsin
Agric. Biol. Chem.
48
2025-2031
1984
Bos taurus, Homo sapiens
-
brenda
Pitts, J.E.; Quinn, D.; Uusitalo, J.; Penttilae, M.
Protein engineering of chymosin and expression in Trichoderma reesei
Food Biotechnol.
19
663-666
1991
Bos taurus
brenda
Strop, P.; Sedlacek, J.; Stys, J.; Kaderabkova, Z.; Blaha, I.; Pavlickova, L.; Pohl, J.; Fabry, M.; Kostka, V.; Newman, M.; Frazao, C.; Shearer, A.; Tickle, I.J.; Blundell, T.L.
Engineering enzyme subsite specificity: preparation, kinetic characterization, and X-ray analysis at 2.0-A resolution of Val111Phe site-mutated calf chymosin
Biochemistry
29
9863-9871
1990
Bos taurus
brenda
Pitts, J.E.; Uusitalo, J.M.; Mantafounis, D.; Nugent, P.G.; Quinn, D.D.; Orprayoon, P.; Penttilae, M.E.
Expression and characterisation of chymosin pH optima mutants produced in Trichoderma reesei
J. Biotechnol.
28
69-83
1993
Bos taurus
brenda
Nugent, P.G.; Albert, A.; Orprayoon, P.; Wilsher, J.; Pitts, J.E.; Blundell, T.L.; Dhanaraj, V.
Protein engineering loops in aspartic proteinases: site-directed mutagenesis, biochemical characterization and X-ray analysis of chymosin with a replaced loop from rhizopuspepsin
Protein Eng.
9
885-893
1996
Bos taurus
brenda
Mantafounis, D.; Pitts, J.
Protein engineering of chymosin; modification of the optimum pH of enzyme catalysis
Protein Eng.
3
605-609
1990
Bos taurus
brenda
Gustchina, E.A.; Majer, P.; Rumsh, L.D.; Ginodman, L.M.; Andreeva, N.S.
Post X-ray crystallographic studies of chymosin specificity. The role of histidine-proline cluster of kappa-casein in catalytic reactions
Adv. Exp. Med. Biol.
436
179-184
1998
Bos taurus
brenda
Kappeler, S.R.; van den Brink, H.J.; Rahbek-Nielsen, H.; Farah, Z.; Puhan, Z.; Hansen, E.B.; Johansen, E.
Characterization of recombinant camel chymosin reveals superior properties for the coagulation of bovine and camel milk
Biochem. Biophys. Res. Commun.
342
647-654
2006
Bos taurus, Camelus dromedarius
brenda
Starovoitova, V.V.; Velichko, T.I.; Baratova, L.A.; Filippova, I.Y.; Lavrenova, G.I.
A comparative study of functional properties of calf chymosin and its recombinant forms
Biochemistry (Moscow)
71
320-324
2006
Bos taurus
brenda
Huppertz, T.; Uniacke, T.; Kelly, A.L.; Fox, P.F.
Inhibition of the proteolytic activity of indigenous plasmin or exogenous chymosin and pepsin in bovine milk by blood serum
Int. dairy J.
16
691-696
2006
Bos taurus
brenda
Moschopoulou, E.E.; Kandarakis, I.G.; Alichanidis, E.; Anifantakis, E.M.
Purification and characterization of chymosin and pepsin from kid
J. Dairy Res.
73
49-57
2006
Bos taurus
brenda
Molle, D.; Jean, K.; Guyomarch, F.
Chymosin sensitivity of the heat-induced serum protein aggregates isolated from skim milk
Int. Dairy J.
16
1435-1441
2006
Bos taurus
brenda
Bansal, N.; Fox, P.F.; McSweeney, P.L.
Aggregation of rennet-altered casein micelles at low temperatures
J. Agric. Food Chem.
55
3120-3126
2007
Bos taurus
brenda
Renan, M.; Guyomarch, F.; Chatriot, M.; Gamerre, V.; Famelart, M.H.
Limited enzymatic treatment of skim milk using chymosin affects the micelle/serum distribution of the heat-induced whey protein/kappa-casein aggregates
J. Agric. Food Chem.
55
6736-6745
2007
Bos taurus
brenda
van den Brink, H.J.; Petersen, S.G.; Rahbek-Nielsen, H.; Hellmuth, K.; Harboe, M.
Increased production of chymosin by glycosylation
J. Biotechnol.
125
304-310
2006
Bos taurus
brenda
Reh, G.; Spelzini, D.; Tubio, G.; Pico, G.; Farruggia, B.
Partition features and renaturation enhancement of chymosin in aqueous two-phase systems
J. Chromatogr. B
860
98-105
2007
Bos taurus
brenda
Palmer, D.S.; Christensen, A.U.; Srensen, J.; Celik, L.; Qvist, K.B.; Schiott, B.
Bovine chymosin: a computational study of recognition and binding of bovine kappa-casein
Biochemistry
49
2563-2573
2010
Bos taurus
brenda
Hidalgo, M.E.; Pires, M.S.; Risso, P.H.
A study on bovine kappa-casein aggregation after the enzymatic action of chymosin
Colloids Surf. B Biointerfaces
76
556-563
2010
Bos taurus
brenda
Kumar, A.; Grover, S.; Sharma, J.; Batish, V.K.
Chymosin and other milk coagulants: sources and biotechnological interventions
Crit. Rev. Biotechnol.
30
243-258
2010
Bos taurus
brenda
Kageyama, H.; Ueda, H.; Tezuka, T.; Ogasawara, A.; Narita, Y.; Kageyama, T.; Ichinose, M.
Differences in the P1' substrate specificities of pepsin A and chymosin
J. Biochem.
147
167-174
2010
Bos taurus (P00794), Bos taurus
brenda
Justesen, S.F.; Lamberth, K.; Nielsen, L.L.; Schafer-Nielsen, C.; Buus, S.
Recombinant chymosin used for exact and complete removal of a prochymosin derived fusion tag releasing intact native target protein
Protein Sci.
18
1023-1032
2009
Bos taurus
brenda
Sorensen, J.; Palmer, D.S.; Qvist, K.B.; Schiott, B.
Initial stage of cheese production: a molecular modeling study of bovine and camel chymosin complexed with peptides from the chymosin-sensitive region of kappa-casein
J. Agric. Food Chem.
59
5636-5647
2011
Bos taurus (P00794), Bos taurus, Camelus dromedarius (Q9GK11)
brenda
Langholm Jensen, J.; Molgaard, A.; Navarro Poulsen, J.C.; Harboe, M.K.; Simonsen, J.B.; Lorentzen, A.M.; Hjerno, K.; van den Brink, J.M.; Qvist, K.B.; Larsen, S.
Camel and bovine chymosin: the relationship between their structures and cheese-making properties
Acta Crystallogr. Sect. D
69
901-913
2013
Bos taurus (P00794), Bos taurus, Camelus dromedarius (Q9GK11)
brenda
Bijl, E.; van Valenberg, H.; Sikkes, S.; Jumelet, S.; Sala, G.; Olieman, K.; van Hooijdonk, T.; Huppertz, T.
Chymosin-induced hydrolysis of caseins: Influence of degree of phosphorylation of alpha-s1-casein and genetic variants of beta-casein
Int. Dairy J.
39
215-221
2014
Bos taurus
-
brenda
Moller, K.K.; Rattray, F.P.; Sorensen, J.C.; Ardoe, Y.
Comparison of the hydrolysis of bovine kappa-casein by camel and bovine chymosin: a kinetic and specificity study
J. Agric. Food Chem.
60
5454-5460
2012
Bos taurus, Camelus dromedarius
brenda
Costabel, L.M.; Bergamini, C.V.; Pozza, L.; Cuffia, F.; Candioti, M.C.; Hynes, E.
Influence of chymosin type and curd scalding temperature on proteolysis of hard cooked cheeses
J. Dairy Res.
85
375-384
2015
Bos taurus
brenda
Jensen, J.L.; Jacobsen, J.; Moss, M.L.; Rasmussen, F.; Qvist, K.B.; Larsen, S.; van den Brink, J.M.
The function of the milk-clotting enzymes bovine and camel chymosin studied by a fluorescence resonance energy transfer assay
J. Dairy Sci.
98
2853-2860
2015
Bos taurus, Camelus dromedarius
brenda
Noseda, D.G.; Blasco, M.; Recupero, M.; Galvagno, M.A.
Bioprocess and downstream optimization of recombinant bovine chymosin B in Pichia (Komagataella) pastoris under methanol-inducible AOXI promoter
Protein Expr. Purif.
104
85-91
2014
Bos taurus
brenda
Belenkaya, S.; Rudometov, A.; Shcherbakov, D.; Balabova, D.; Kriger, A.; Belov, A.; Koval, A.; Elchaninov, V.
Biochemical properties of recombinant chymosin in alpaca (Vicugna pacos L.)
Appl. Biochem. Microbiol.
54
569-576
2018
Bos taurus, Vicugna pacos
-
brenda
Rayanatou, I.A.; Mahamadou, E.G.; Garric, G.; Harel-Oger, M.; Leduc, A.; Jardin, J.; Briard-Bion, V.; Cauty, C.; Adakal, H.; Grongnet, J.F.; Gaucheron, F.
Physico-chemical characterization of dairy gel obtained by a proteolytic extract from Calotropis procera - A comparison with chymosin
Food Chem.
232
405-412
2017
Bos taurus
brenda
Wei, Z.Y.; Zhang, Y.Y.; Wang, Y.P.; Fan, M.X.; Zhong, X.F.; Xu, N.; Lin, F.; Xing, S.C.
Production of bioactive recombinant bovine chymosin in tobacco plants
Int. J. Mol. Sci.
17
E624
2016
Bos taurus
brenda
Rolet-Repecaud, O.; Arnould, C.; Dupont, D.; Gavoye, S.; Beuvier, E.; Achilleos, C.
Development and evaluation of a monoclonal antibody-based inhibition ELISA for the quantification of chymosin in solution
J. Agric. Food Chem.
63
4799-4804
2015
Bos taurus
brenda
Ansari, S.M.; Coletta, A.; Kirkeby Skeby, K.; Sorensen, J.; Schiott, B.; Palmer, D.S.
Allosteric-activation mechanism of bovine chymosin revealed by bias-exchange metadynamics and molecular dynamics simulations
J. Phys. Chem. B
120
10453-10462
2016
Bos taurus (P00794), Bos taurus
brenda
Leite Junior, B.; Tribst, A.; Cristianini, M.
The effect of high pressure processing on recombinant chymosin, bovine rennet and porcine pepsin Influence on the proteolytic and milk-clotting activities and on milk-clotting characteristics
LWT-Food Sci. Technol.
76
351-360
2017
Bos taurus
-
brenda
Espinoza-Molina, J.A.; Acosta-Muniz, C.H.; Sepulveda, D.R.; Zamudio-Flores, P.B.; Rios-Velasco, C.
Codon optimization of the "Bos taurus Chymosin" gene for the production of recombinant chymosin in Pichia pastoris
Mol. Biotechnol.
58
657-664
2016
Bos taurus
brenda
Ulusu, Y.; Sentuerk, S.B.; Kudug, H.; Goekce, I.
Expression, purification, and characterization of bovine chymosin enzyme using an inducible pTOLT system
Prep. Biochem. Biotechnol.
46
596-601
2016
Bos taurus
brenda
Ansari, S.M.; Sorensen, J.; Schiott, B.; Palmer, D.S.
On the effect of mutations in bovine or camel chymosin on the thermodynamics of binding kappa-caseins
Proteins
86
75-87
2018
Bos taurus (P00794), Bos taurus, Camelus dromedarius (Q9GK11)
brenda