Comparative study of the inactivation kinetics of pectinmethylesterase in tomato juice and purified form

被引：72

作者：

Fachin, D ^{[1
]}

Van Loey, AM ^{[1
]}

Nguyen, BL ^{[1
]}

Verlent, I ^{[1
]}

Indrawati ^{[1
]}

Hendrickx, ME ^{[1
]}

机构：

[1] Katholieke Univ Leuven, Dept Food & Microbial Technol, Lab Food Technol, B-3001 Louvain, Belgium

来源：

BIOTECHNOLOGY PROGRESS | 2002年 / 18卷 / 04期

关键词：

D O I：

10.1021/bp0155080

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：

Pectinmethylesterase (PME) extracted from tomato fruit was purified by affinity chromatography. A single peak of PME activity was observed, presenting a molar mass of 33.6 kDa, an isoelectric point higher than 9.3, and an optimal temperature and pH for activity of 55 degreesC and 8.0, respectively. The processing stability of purified tomato PME in buffer solution was compared to PME stability in tomato juice. In both media, thermal inactivation of PME presented first-order inactivation kinetics, PME in tomato juice being more heat-labile than purified PME. Regarding high-pressure treatment, tomato PME showed to be very pressure-resistant, revealing an outspoken antagonistic effect of,temperature and pressure. To avoid cloud loss in tomato juice, a time-temperature treatment of 1 min at 76.5 degreesC was calculated in order to have a residual PME activity of 1 x 10(-4) U/mL.

引用

页码：739 / 744

页数：6

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