PECTIN LYASE FROM ASPERGILLUS SP CH-Y-1043

被引:27
作者
DELGADO, L [1 ]
TREJO, BA [1 ]
HUITRON, C [1 ]
AGUILAR, G [1 ]
机构
[1] NATL AUTONOMOUS UNIV MEXICO,INST BIOMED RES,DEPT BIOTECHNOL,MEXICO CITY 04510,DF,MEXICO
关键词
D O I
10.1007/BF00205043
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Aspergillus sp. CH-Y-1043 synthesizes pectin lyase when grown on citrus pectin at 37-degrees-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-degrees-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-degrees-C it preserves more than 95% of its activity at pHs ranging from 2.0 to 10.0, and at 30-degrees-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-degrees-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.
引用
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页码:515 / 519
页数:5
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