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PubMed · 2484752

Microbial amylases.

P Cornelis
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Abstract

Amylases are of tremendous importance in the food industry. Different enzymes used separately or together convert starch into glucose, maltose, dextrins or cyclodextrins. Most enzymes of industrial importance are of microbial origin, and the list of amylases produced by molecular cloning is rapidly expanding.

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AmylasesBacteriaCloning, MolecularJournal ArticleReview

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BibTeXRIS

P Cornelis. 1987. Microbial amylases.. https://pubmed.ncbi.nlm.nih.gov/2484752/

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PubMed1992

Effects of calyculin A on amylase release in streptolysin-O permeabilized acinar cells.

The effects of the phosphatase inhibitors calyculin A and okadaic acid on amylase release from streptolysin-O permeabilized rat pancreatic acini were investigated. Both agents induced similar biphasic effects with moderate potentiation of calcium-stimulated amylase release at medium and strong inhibition at higher concentrations. Calyculin A was thirty times more potent than okadaic acid and at 100 nM totally inhibited calcium-induced amylase release while 3 microM okadaic acid reduced amylase release by 78%. 100nM calyculin A also completely inhibited GTP gamma S-potentiated amylase release and partially inhibited phorbol ester potentiated secretion. The data indicate that inhibition of a serine/threonine phosphatase, probably a type 1 phosphatase, leads to inhibition of calcium-induced amylase release in permeabilized pancreatic acini.

Amylases↗