Abstract
Calf chymosin was shown to catalyse peptide synthesis optimally over the range pH 4-5, giving satisfactory yields of methyl esters or p-nitroanilides of benzyloxycarbonyl tetra- to hexa-peptides, provided that hydrophobic amino-acid residues form the new peptide bonds. The effectiveness of the enzyme depends also on the nature of adjacent amino-acid residues. As an aspartate-proteinase with a characteristic specificity pattern chymosin would be useful for the synthesis of middle-length peptides.
Full text
PDF


Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Abdel Malak C., Filippova I. Y., Lysogorskaya E. N., Anisimova V. V., Lavrenova G. I., Stepanov V. M. Pepsin as a catalyst of peptide synthesis. Enzyme co-precipitation with emerging peptide products. Int J Pept Protein Res. 1992 May;39(5):443–449. doi: 10.1111/j.1399-3011.1992.tb01448.x. [DOI] [PubMed] [Google Scholar]
- DELFOUR A., JOLLES J., ALAIS C., JOLLES P. CASEINO-GLYCOPEPTIDES: CHARACTERIZATION OF A METHIONINE RESIDUE AND OF THE N-TERMINAL SEQUENCE. Biochem Biophys Res Commun. 1965 May 3;19:452–455. doi: 10.1016/0006-291x(65)90145-2. [DOI] [PubMed] [Google Scholar]
- Foltmann B., Szecsi P. B., Tarasova N. I. Detection of proteases by clotting of casein after gel electrophoresis. Anal Biochem. 1985 May 1;146(2):353–360. doi: 10.1016/0003-2697(85)90551-2. [DOI] [PubMed] [Google Scholar]
- Fruton J. S. Proteinase-catalyzed synthesis of peptide bonds. Adv Enzymol Relat Areas Mol Biol. 1982;53:239–306. doi: 10.1002/9780470122983.ch7. [DOI] [PubMed] [Google Scholar]
- Hill R. D. The nature of the rennin-sensitive bond in casein and its possible relation to sensitive bonds in other proteins. Biochem Biophys Res Commun. 1968 Nov 25;33(4):659–663. doi: 10.1016/0006-291x(68)90346-x. [DOI] [PubMed] [Google Scholar]
- Mantafounis D., Pitts J. Protein engineering of chymosin; modification of the optimum pH of enzyme catalysis. Protein Eng. 1990 Jul;3(7):605–609. doi: 10.1093/protein/3.7.605. [DOI] [PubMed] [Google Scholar]
- Martin P., Raymond M. N., Bricas E., Dumas B. R. Kinetic studies on the action of Mucor pusillus, Mucor miehei acid proteases and chymosins A and B on a synthetic chromophoric hexapeptide. Biochim Biophys Acta. 1980 Apr 11;612(2):410–420. doi: 10.1016/0005-2744(80)90124-2. [DOI] [PubMed] [Google Scholar]
- Raymond M. N., Garnier J., Bricas E. Studies on the specificity of chymosin (rennin). I. Kinetic parameters of the hydrolysis of synthetic oligopeptide substrates. Biochimie. 1972;54(2):145–154. doi: 10.1016/s0300-9084(72)80098-1. [DOI] [PubMed] [Google Scholar]
- Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun. 1967 Apr 20;27(2):157–162. doi: 10.1016/s0006-291x(67)80055-x. [DOI] [PubMed] [Google Scholar]
- Visser S., Van Rooijen P. J., Schattenkerk C., Kerling K. E. Peptide substrates for chymosin (rennin). Kinetic studies with peptides of different chain length including parts of the sequence 101-112 of bovine k-casein. Biochim Biophys Acta. 1976 Jun 7;438(1):265–272. doi: 10.1016/0005-2744(76)90242-4. [DOI] [PubMed] [Google Scholar]
