Activation and conformational changes of chitinase induced by ultrasound

被引：28

作者：

Hou, Furong ^{[1
]}

Ma, Xiaobin ^{[1
]}

Fan, Lihua ^{[1
]}

Wang, Danli ^{[1
]}

Wang, Wenjun ^{[1
]}

Ding, Tian ^{[1
,3
]}

Ye, Xingqian ^{[1
,2
,3
]}

Liu, Donghong ^{[1
,2
,3
]}

机构：

[1] Zhejiang Univ, Coll Biosyst Engn & Food Sci, 866 Yuhangtang Rd, Hangzhou 310058, Zhejiang, Peoples R China

[2] Zhejiang Univ, Fuli Inst Food Sci, Hangzhou 310058, Zhejiang, Peoples R China

[3] Zhejiang R&D Ctr Food Technol & Equipment, Zhejiang Key Lab Agrofood Proc, Hangzhou 310058, Zhejiang, Peoples R China

来源：

FOOD CHEMISTRY | 2019年 / 285卷

关键词：

Chitinase; Ultrasound; Enzymatic kinetics; Conformational changes; BETA-N-ACETYLGLUCOSAMINIDASE; POLYPHENOL OXIDASE; CELLULASE; PURIFICATION; PRESSURE; KINETICS; ENZYMES; SYSTEM;

D O I：

10.1016/j.foodchem.2019.01.180

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

This study investigated the effect of ultrasound on chitinase activity and conformational changes. Results revealed that ultrasound activated chitinase with a maximum enhancement of 19.17% compared with the untreated chitinase. Furthermore, an increase of V-max and a decrease of K-m after sonication were obtained, illustrating that the affinity between chitinase and substrate was intensified. No obvious effect on the tolerance to most metal ions was exhibited whether sonicated or not (p > 0.05). The conformational changes of chitinase were analyzed by circular dichroism (CD), Fourier transform infrared (FTIR), Raman and fluorescence spectroscopy. Results indicated that the activation of chitinase induced by ultrasound was presumably due to the decrease of tryptophan on the chitinase surface and the increase of beta-sheet and random coil in chitinase secondary conformation. In brief, ultrasound is a possible way to activate chitinase to increase its application in food industry.

引用

页码：355 / 362

页数：8

共 41 条

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