摘要
毛霉蛋白酶可以高效地水解大豆蛋白,而且对蛋白水解物具有良好的脱苦效果.为了开发这一蛋白酶系,采用离子交换、疏水层析及凝胶层析等方法,从雅致放射毛霉AS3.2778的发酵麸曲中分离纯化出一蛋白酶组分,并对其水解特性进行了探讨.结果显示：纯化后的蛋白酶是一单体蛋白,其相对分子质量大约为32000;该蛋白酶在55℃、pH8.0-10.0的条件下对大豆蛋白显示出较强的水解能力,其水解效果明显优于商品化的蛋白酶（如木瓜蛋白酶、Alcalase及Protamex）,表明该蛋白酶比以上几种商品化蛋白酶具有更广泛的肽键选择性,对大豆蛋白亲和力更强,在大豆蛋白肽链上有相对较多的酶切位点.
The proteases from mucor is of relatively high hydrolysis efficiency to soy protein and of good debittering effect to the hydrolysates of protein. In order to effectively explore such proteases, one protease was purified from the fermented wheat bran by Actinomucor elegans AS3. 2778 using ion exchange chromatography, hydrophobic chromatography, and gel chromatography, and its hydrolysis properties to soybean protein were investigated. The results show that the purified protease is a single-chain polypeptide with a relative molecular mass of 32000, which has relatively higher hydrolysis activity to soy protein at 55 ℃ and pH8.0 - 10. 0 than such commercial proteases as papain, Alcalase and Protamex. It is thus concluded that, as compared with the above-mentioned commercial proteases, the purified protease is of more extensive peptide-bond selectivity, stronger affinity to soybean protein isolate （SPI）, and more cleavage points on SPI.
出处
《华南理工大学学报（自然科学版）》
EI
CAS
CSCD
北大核心
2008年第12期106-111,共6页
Journal of South China University of Technology(Natural Science Edition)
基金
广东省自然科学基金资助项目(06300197)
广东省科技计划项目(2006A10602001)
广州市科技攻关项目(2006Z3-E0701)
关键词
雅致放射毛霉
蛋白酶
纯化
水解
Actinomucor elegans
protease
purification
hydrolysis
