4.4 Article Proceedings Paper

Exploring and exploiting starch-modifying amylomaltases from thermophiles

期刊

BIOCHEMICAL SOCIETY TRANSACTIONS
卷 32, 期 -, 页码 279-282

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PORTLAND PRESS LTD
DOI: 10.1042/BST0320279

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amylomaltase; enzyme; gel; 4-alpha gluwcanotranslerase; glycosidic linkage; starch

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Starch is a staple food present in water-insoluble granules in many economically important crops. It is composed of two glucose polymers: the linear alpha-1,4-linked amylose and amylopectin with a backbone of alpha-1,4-glycosidic bonds and alpha-1,6-linked side chains. To dissolve starch completely in water it needs to be heated; when it cools down too much the starch solution forms a thermo-irreversible gel. Amylomaltases (EC 2.4.1.25) are enzymes that transfer a segment of an alpha-1,4-D-glucan to a new 4-position in an acceptor, which may be glucose or another alpha-1,4-D-glucan. Acting upon starch, amylomaltases can produce cycloamylose or a thermoreversible starch gel, both of which are of commercial interest.

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