Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 2483-2492 |
| Number of pages | 10 |
| Journal | Biotechnology and Bioengineering |
| Volume | 23 |
| Issue number | 11 |
| DOIs | |
| State | Published - Nov 1981 |
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