Degradation of inactivated alpha-amylase by associated proteases
Ulbrich, R.; Kvesitadze, G.; Schellenberger, A.
Acta Biologica et Medica Germanica 41(6): 509-513
1982
ISSN/ISBN: 0001-5318 PMID: 6183852 Document Number: 183818
Alpha-Amylase preparations often contain small quantities of proteolytic activity which are difficult to remove. On the example of fungal alpha-amylase, such associated proteases have been shown to possess a specific activity to the denatured amylase molecules. The amylase is not attacked under native conditions, whereas in the thermal denaturation a rapid degradation of only the inactivated molecules occurs. A specific metabolic function of these associated proteases in the return of denatured amylase molecules to the amino acid pool is suggested.