Some biochemical properties of polyphenol oxidase from two varieties of avocado

被引:65
作者
Gómez-López, VM [1 ]
机构
[1] Cent Univ Venezuela, Fac Ciencias, Inst Ciencia & Tecnol Alimentos, Caracas 1041A, Venezuela
关键词
polyphenol oxidase; avocado; enzymatic browning; Persea americsna; tropical fruit;
D O I
10.1016/S0308-8146(01)00331-4
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
A study of crude polyphenol oxidases from two avocado (Persea americana Mill.) varieties, Booth 1 (BIPPO) and Julio Millan (JMPPO), were carried out to provide information useful for guiding food processing operations. Results are reported as "apparent" data because crude extracts were used, activities of which can be derived from a combination of isoenzymes. The pH-activity optimum was pH 7.5-7.6 for both extracts. Heat inactivation, between 67 and 84 degreesC was biphasic with activation energies ranging from 21.4 to 64.1 kcal/mol. The apparent substrate specificity was established from values V-max/K-m as: 4-methyl catechol > chlorogenic acid > pyrogallol > catechol > caffeic acid > DL-DOPA for BIPPO. The substrate specificity for JMPPO was: 4-methyl catechol > chlorogenic acid > pyrogallol > caffeic acid > catechol > DL-DOPA > protocatechuic acid. The order of inhibitor effectiveness was: L-cysteine > ascorbic acid > resorcinol > glycine >NaCl. (C) 2002 Elsevier Science Ltd. All rights reserved.
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页码:163 / 169
页数:7
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