Pectin lyase from Aspergillus sp. CH-Y-1043 |
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Authors: | Luis Delgado Blanca A Trejo Carlos Huitrón Guillermo Aguilar |
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Institution: | (1) Department of Biotechnology, Institute of Biomedical Research, National University of Mexico, UNAM, A. P. 70228, D. F. 04510 México, Mexico;(2) Present address: Department of Food Science and Biotechnology, Faculty of Chemical Sciences, National University of Mexico, UNAM, Ciudad Universitaria, C. P. 04510 Mexico, D. F. Mexico |
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Abstract: | Aspergillus sp. CH-Y-1043 synthesizes pectin lyase when grown on citrus pectin at 37° C. Production is favoured by increased esterification degree of the pectin used as carbon source. This enzyme displays higher activity at pH values of 8.5–8.8 and temperatures of 40–45° C. The optimal substrate for the enzyme was highly esterified pectin and no enzymatic activity was registered on polygalacturonic acid. The activity is stimulated by, though not dependent on, divalent cations (Ca2+, Mg2+, Mn2+, Ba2+ and Co2+) and inhibited by Zn2+, and it is not sensitive to the addition of EDTA. The enzyme is very stable when exposed to pH variations: at 4° C it preserves more than 95% of its activity at pHs ranging from 2.0 to 10.0, and at 30° C stability is preserved at pHs ranging from 4.0 to 8.0. At a constant pH of 5.0, the enzyme conserves its stability at temperatures ranging from 4 to 50° C and at pH 8.0 sensitivity to temperature increased. The results on the endo-exo nature of the enzyme suggest that this is an exo-pectin lyase.
Correspondence to: G. Aguilar |
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