Milk Proteins 1971
DOI: 10.1016/b978-0-12-485202-0.50011-7
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The Biochemistry of Prorennin (Prochymosin) and Rennin (Chymosin)

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Cited by 20 publications
(9 citation statements)
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“…In order to investigate whether the production levels of heterologous proteins were improved in the Aovps10 gene disruptant NSlDv10, we constructed strains expressing CHY, as a model protein. The initial translation product of CHY, prochymosin, contains a 42-amino-acid Nterminal sequence which is automatically cleaved at low pH to yield active chymosin (7,8). A. oryzae ␣-amylase (AmyB) was used as the carrier protein for fusion with CHY since such fusions have been shown to aid the successful production of heterologous proteins (15,16,31).…”
Section: Resultsmentioning
confidence: 99%
“…In order to investigate whether the production levels of heterologous proteins were improved in the Aovps10 gene disruptant NSlDv10, we constructed strains expressing CHY, as a model protein. The initial translation product of CHY, prochymosin, contains a 42-amino-acid Nterminal sequence which is automatically cleaved at low pH to yield active chymosin (7,8). A. oryzae ␣-amylase (AmyB) was used as the carrier protein for fusion with CHY since such fusions have been shown to aid the successful production of heterologous proteins (15,16,31).…”
Section: Resultsmentioning
confidence: 99%
“…Chymosin, an aspartyl protease produced in the abomasum of young ruminants, is the preferred milk clotting protease for cheese manufacture (Foltmann, 1971). The isoelectric point is 4.6 and chymosin stability is greatest at about pH 2 and between pH 5 and 6.5.…”
Section: Introductionmentioning
confidence: 99%
“…Chymosin catalyses specific cleavage of the PHE 105 -MET 106 bond of -casein, destabi-lizing the casein micelle and causing precipitation. The initial translation product, prochymosin, contains a 42 amino acid N terminal sequence which is cleaved to yield active chymosin (Foltmann, 1971). Both recombinant prochymosin (Emtage et al, 1983;Goff et al, 1984) and chymosin (Dunn-Colemann et al, 1991;Harkki et al, 1989) have been produced.…”
Section: Introductionmentioning
confidence: 99%
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“…The sequence of the remaining part of the molecule was established after a second tryptic digestion of the demaleylated peptide, from which the two basic peptides Tm-2, t-2 and Tm-2, t-3 were isolated. An overlapping sequence of the peptides Tm-1 and Tm-2 has eventually been provided by a peptide (AP-Cl) which has been isolated from a chymotryptic digest of activation peptides liberated during the conversion of prochymosin into chymosin [9].…”
Section: Methodsmentioning
confidence: 99%