Alginic Acid Degradation by Eliminases from Abalone Hepatopancreas

Two separate alginic acid eliminases have been purified from abalone hepatopancreas. Alginase I appeared to be specific for β-1,4 bonds involving d -mannuronic acid units and apperently acts at random on internal bonds. Alginase II appeared to cleave 1,4 bonds involving l -guluronic acid and to wor...

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Bibliographic Details
Published inThe Journal of biological chemistry Vol. 242; no. 5; pp. 845 - 851
Main Authors Nakada, H I, Sweeny, P C
Format Journal Article
LanguageEnglish
Published United States American Society for Biochemistry and Molecular Biology 10.03.1967
Subjects
Alginates - metabolism
Animals
Chemical Phenomena
Chemistry, Physical
Chlorides
Chromatography, Paper
Glycoside Hydrolases - metabolism
In Vitro Techniques
Liver - enzymology
Mollusca
Pancreas - enzymology
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Summary:Two separate alginic acid eliminases have been purified from abalone hepatopancreas. Alginase I appeared to be specific for β-1,4 bonds involving d -mannuronic acid units and apperently acts at random on internal bonds. Alginase II appeared to cleave 1,4 bonds involving l -guluronic acid and to work at or near chain ends. A combination of both enzymes could not degrade alginic acid completely, indicating the presence of other types of bonds. An ionic concentration of about 50 to 75 m m was required for maximum activity. It appears that the high ionic strength was necessary to remove bound water from the substrate, alginic acid, and to neutralize the negative charges on the polyanion in order to render the molecular configuration more suitable for enzyme action.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(18)96201-0