J Integr Plant Biol. ›› 2001, Vol. 43 ›› Issue (11): 1150-1153.

• Research Articles • Previous Articles     Next Articles

A Proteinase from Mung Bean Sprouts That Inactivaties Soybean Trypsin Inhibitor (in English)

CHEN Zhong, Yang Xiao-Quan and ZHAO Mou-Ming   


By 30%-60% (NH4)2SO4 fractional precipitation, anion-exchange chromatography on DEAE-Sepharose CL-6B, gel filtration on Sephacryl S-200 and anion-exchange chromatography on Waters AP-1 column (ProteinPM-Pak DEAE 15HR), a proteinase which can inactivate soybean trypsin inhibitor (STI) was purified from mung bean (Vigna rabiata (L.) Wilczek) sprouts. Its molecular weight was estimated to be 29.8 kD by SDS-PAGE, and its Km and Vmax for STI were 769.2N-α-benzoyl-L-arginine ethyl ester BAEE/mL and 115.3 BAEE·mL-1·min-1 respectively. This proteinase was stable at temperatures lower than 50℃ and pH 6.5-8.5, and 90.91% STI activity of defatted soybean powder was inactivated by this preparation, with proteolytic activity 5 000 BAEE/mL at 50℃ and pH 8.0 in 4 h.

陈中 杨晓泉 赵谋明

摘要: 通过30%-60%(NH4)2SO4分级沉淀、DEAE-Sepharose CL-6B离子交换层析、Sephacryl S-200凝胶过滤层析和Waters AP-1离子交换层析,从萌发的绿豆(Vigna rabiata(L.)Wilczek)种子中分离纯化出一种可降解大豆胰蛋白酶抑制剂(STI)的蛋白酶。SDS-PAGE测定该酶的分子量为29.8kD。该酶催化降解STI的Km值为769.2BAEE/mL,Vmax为115.3BAEE·min^-1。该酶在50℃、pH8.0,相对酶活力5000BAEE/mL和4h的反应时可将脱脂大豆粉中的STI活性钝化90.91%。该酶在温度低于50℃及pH6.5-8.5时能保持其活性。

关键词: 蛋白酶;钝化;大豆胰蛋白酶抑制剂

Key words: proteinase, inactivate, soybean trypsin inhibitor

Editorial Office, Journal of Integrative Plant Biology, Institute of Botany, CAS
No. 20 Nanxincun, Xiangshan, Beijing 100093, China
Tel: +86 10 6283 6133 Fax: +86 10 8259 2636 E-mail: jipb@ibcas.ac.cn
Copyright © 2022 by the Institute of Botany, the Chinese Academy of Sciences
Online ISSN: 1744-7909 Print ISSN: 1672-9072 CN: 11-5067/Q