Purification and characterization of polygalacturonase from banana fruit

被引：30

作者：

Pathak, N ^{[1
]}

Mishra, S ^{[1
]}

Sanwal, GG ^{[1
]}

机构：

[1] Univ Lucknow, Dept Biochem, Lucknow 226007, Uttar Pradesh, India

来源：

PHYTOCHEMISTRY | 2000年 / 54卷 / 02期

关键词：

Musa acuminata; Musaceae; banana; enzyme purification; isoenzyme; polygalacturonase;

D O I：

10.1016/S0031-9422(00)00061-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Polygalacturonase isoenzyme 3 (PG-3) was purified to homogeneity with a specific activity of 0.7 mu katal mg(-1) protein from banana fruit pulp. The purified enzyme was a glycoprotein with ca. 8% carbohydrate. The molecular weight of the native enzyme was found to be 90 +/- 10 kDa with a subunit molecular weight of 29 +/- 2 kDa. The enzyme exhibited optimum activity at pH 4.3 and temperature 40 degrees C with activation energy 35.4 kJ mol(-1). A unique property of the enzyme was the requirement of SH groups for the enzyme activity. The enzyme was inhibited by p-CMB and activated by 2-ME and DTT. The inhibition of p-CMB could be reversed by DTT. The enzyme contained eight free -SH groups. The K-m of the enzyme was 0.15% for polygalacturonic acid. (C) 2000 Elsevier Science Ltd. All rights reserved.

引用

页码：147 / 152

页数：6

共 25 条

[1] CELL-WALL METABOLISM IN RIPENING FRUIT .1. CELL-WALL CHANGES IN RIPENING BARTLETT PEARS [J].