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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.