A trypsin inhibitor from Cassia obtusifolia seeds: isolation, characterization and activity against Pieris rapae

被引:0
|
作者
Hai Liao
Wei Ren
Zhuang Kang
Jia-Hong Jiang
Xiao-Jun Zhao
Lin-Fang Du
机构
[1] Sichuan University,College of Life Science
[2] Southwest Jiaotong University,College of Pharmacy
[3] Sichuan University,Institute for Nanobiomedical Technology and Membrane Biology
来源
Biotechnology Letters | 2007年 / 29卷
关键词
Isolation; Pest control; Trypsin inhibitor;
D O I
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中图分类号
学科分类号
摘要
A trypsin inhibitor was isolated from Cassia obtusifolia by ammonium sulfate precipitation, Sepharose 4B-trypsin affinity and Sephadex G-75 chromatography. The inhibitor consisted of a single polypeptide chain with a molecular mass of 19, 812.55 Da. It was stable from pH 2 to 12 for 24 h, whereas it was unstable either above 70°C for 10 min or under reduced conditions. The inhibitor, which inhibited trypsin activity with an apparent Ki of 0.3 μM, had one reactive site involving a lysine residue. The native inhibitor was resistant to pepsin digestion, whereas the heated inhibitor produced 40% degree of susceptibility. The disulfide linkage and lysine residue were important in maintaining its conformation. Partial amino acid sequence of the purified protein showed a high degree of homology with various members of the Kunitz inhibitor family. Moreover, the inhibitor showed significant inhibitory activity against trypsin-like proteases present in the larval midgut on Pieris rapae and could suppress the growth of larvae.
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页码:653 / 658
页数:5
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