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Further purification and characterization of a thermophilic rennet
Author(s) -
Laxer Shoshana,
Pnsky Alex,
Bartoov Benjamin
Publication year - 1981
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260231108
Subject(s) - rennet , chemistry , thermophile , skimmed milk , trypsin , chromatography , size exclusion chromatography , fermentation , pepsin , filtration (mathematics) , chymosin , chymotrypsin , ion exchange , enzyme , food science , biochemistry , casein , organic chemistry , ion , statistics , mathematics
Further work on a thermophilic rennet synthesized by a thermophilic actinomycete is reported. It was produced by growth in fermentor of 50‐or‐200‐L volume and was purified by membrane filtration of a cell‐free supernatant and then molecular filtration and ion exchange chromatography. Its stability under various conditions was determined: The enzyme is a true rennet requiring calcium ions for activity. Experiment shows that it resembles neither pepsin, trypsin, nor chymotrypsin. It is freeze‐labile with a molecular weight of 9700 from amino acid composition. When skim milk powder was added to the growth medium, a rennet with different properties was obtained.