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机构地区:[1]山西大学生物技术研究所,化学生物学与分子工程教育部重点实验室,山西太原030006
出 处:《食品工业科技》2009年第5期148-150,157,共4页Science and Technology of Food Industry
基 金:山西省重点实验室开放基金(20063003);太原市大学生创新创业计划(08122054)
摘 要:以硅胶为载体,戊二醛为交联剂,进行了胰蛋白酶固定化的研究。以光度比色法测定蛋白酶活力为指标,优化了戊二醛浓度、pH和酶用量等固定化参数,研究了固定化酶的基本特性、最适作用温度和pH及其对酪蛋白的酶解。结果表明:经优化,制备功能化载体的戊二醛最适浓度为1%,固定化pH为8·0,酶与载体比例为50mg/g。固定化胰蛋白酶比活力为4·89×105U/g,最适作用温度和pH范围分别为60℃和6·0~10·0。50℃水解酪蛋白,水解60min,重复使用8次,回收酶活力约为90%。Trypsin was immobilized on the silica gel using glutaraldehyde as cross linker.The concentration of glutaraldehyde, pH and amounts of enzyme were optimized by means of colorimetry.The basic characteristic of immobilized trypsin, optimum reaction temperature, pH and the effects on the hydrolysis of casein were studied.The results showed that the optimum concentration of glutaraldehyde and pH were 1% and 8.0 respectively,the coupling capacity of trypsin was 50mg/g silica gel.And the activity of immobilized trypsin reached 4.89 × 10^5U/g,the optimal temperature and the range of pH were 60℃ and 6.0-10.0.Casein was hydrolyzed by immobilized trypsin lasting 60min under 50℃.The activity yield of the immobilized trypsin was about 90% after 8 cycles reactions.
分 类 号:TS201.25[轻工技术与工程—食品科学]
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