The Isolation and Characterization of an a,4 (4,5 Dehydrogalacturonosyl) Galacturonate Hydrolase | Zendy

NAGEL C. W. | Zendy; HASEGAWA S. | Zendy

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The Isolation and Characterization of an a,4 (4,5 Dehydrogalacturonosyl) Galacturonate Hydrolase

Author(s) -

NAGEL C. W.,

HASEGAWA S.

Publication year - 1968

Publication title -

journal of food science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.772

H-Index - 150

eISSN - 1750-3841

pISSN - 0022-1147

DOI - 10.1111/j.1365-2621.1968.tb03633.x

Subject(s) - tetramer , trimer , dimer , chemistry , pentamer , hydrolase , enzyme , glycosidic bond , stereochemistry , biochemistry , organic chemistry

SUMMARY– An unsaturated oligogalacturonate hydrolase was isolated from the cell extracts of a Bacillus sp. This enzyme attacked only the a 1,4 glycosidic bond adjacent to the terminal 4,5dehydrogalacturonate of unsaturated oligogalacturonides and preferentially attacked short chain unsaturated uronides. The rate of activity was maximal with unsaturated dimer followed by trimer (65% that of dimer), tetramer (47%) and pentamer (35%). The pH optimum was 6.3 to 6.6 and the enzyme did not require calcium ions for its activity. The enzyme was relatively stable below 30°C but lost 90% of its activity after 10 min at 40°C.

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