The Isolation and Characterization of an a,4 (4,5 Dehydrogalacturonosyl) Galacturonate Hydrolase |
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| Authors: | C W NAGEL S HASEGAWA |
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| Affiliation: | Food Science Program, Department of Horticulture, Washington State University, Pullman, Washington 99163 |
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| Abstract: | 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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