Enzymatic activities of maxilact
Nineteen enzymatic activities of Maxilact 20.000 have been assayed using the API ZYM micromethod. Some of them have been found to be positive and these have been studied in more detail. Hydrolysis of lactulose by the action of β-galactosidase is slower than that of lactose. Proteolytic activity has been found in both the soluble and insoluble fractions of Maxilact. Optimum temperature and pH are 45°C and 7, respectively. The action of Maxilact on casein did not alter β-casein, but degraded αs-casein to give a peptide with electrophoretic mobility similar to that produced by the action of rennet. A weak lipolytic activity on tributyrine was also detected.
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| Main Authors: | , , |
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| Format: | artículo biblioteca |
| Published: |
Elsevier
1983-01
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| Online Access: | http://hdl.handle.net/10261/256770 |
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