Abstract：
:Bovine chymosin, an aspartyl protease extracted from abomasum of suckling calves, is synthesized in vivo as preprochymosin and secreted as prochymosin which is autocatalytically activated to chymosin. Chymosin is bilobular, with Asp 32 and Asp 215 acting as the catalytic residues. Chymosin A and chymosin B have pH optima of 4.2 and 3.8, respectively, and act to initiate milk clotting by cleaving kappa-casein between Phe 105 and Met 106. The gene encoding chymosin has been cloned and expressed in suitable bacteria and yeast hosts under the control of lac, trp, trp-beta, gly A genes, and serine hydroxymethyl-transferase promoters. Protein engineering of chymosin has also been attempted. A number of companies are now producing recombinant chymosin for commercial use in cheese manufacture.
journal_name
Biotechnol Advjournal_title
Biotechnology advancesauthors
Mohanty AK,Mukhopadhyay UK,Grover S,Batish VKdoi
10.1016/s0734-9750(99)00010-5subject
Has Abstractpub_date
1999-09-01 00:00:00pages
205-17issue
2-3eissn
0734-9750issn
1873-1899pii
S0734975099000105journal_volume
17pub_type
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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更新日期：2014-01-01 00:00:00
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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pub_type： 杂志文章,评审
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
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journal_title：Biotechnology advances
pub_type： 杂志文章,评审
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