HYDROLYSIS OF THE OLIGOGALACTURONIDES AND PECTIC ACID BY YEAST POLYGALACTURONASE
نویسندگان
چکیده
منابع مشابه
Hydrolysis of the oligogalacturonides and pectic acid by yeast polygalacturonase.
Yeast polygalacturonase (YPG) is a constitutive type enzyme, produced exocellularly and free of pectinesterase by Saccharomyces jragilis (1). It has an optimal pH of 4.4 and appears to be specific in its activity towards polygalacturonides (2). YPG differs from preparations of commercial fungus polygalacturonase in that it cannot carry out a complete breakdown of pectic acid to galacturonic aci...
متن کاملOn the mechanism of action of yeast endo-polygalacturonase on oligogalacturonides and their reduced and oxidized derivatives.
Yeast polygalacturonase catalyzes a random hydrolysis of pectic acid to a mixture of digalacturonic and galacturonic acids via a series of oligogalacturonides (1). This enzyme will be termed yeast endo-polygalacturonase to differentiate it from end group-hydrolyzing enzymes, which have been named exopolygalacturonases (2). Evidence has been presented that yeast endo-polygalacturonase is a singl...
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چکیده ندارد.
15 صفحه اولOxidized oligogalacturonides activate the oxidation of indoleacetic Acid by peroxidase.
Partial hydrolysis of polygalacturonic acid with a purified alpha-1,4-endopolygalacturonase yielded oligogalacturonides and trace amounts of a series of modified oligogalacturonides. Three of the minor products were isolated and identified as oxidized oligogalacturonides possessing termini of galactaric acid. Oxidation of indole-3-acetic acid by peroxidases was activated by oxidized oligogalact...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1954
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)65463-8