摘要
豆壳过氧化物酶(Soybean Hull Peroxidase,SHP)是从大豆豆壳分离得到的一类重要的氧化还原酶,试验通过缓冲溶液抽提法提纯豆壳过氧化物酶,采用愈创木酚法测定酶活力。结果表明,豆壳过氧化物酶是一种耐高温、耐酸碱的酶,其酶作用的最适温度为35℃,最适pH值为5.2,对愈创木酚和过氧化氢的表观Km值分别为1.53 mmol/L和0.36 mmol/L。常见化合物对豆壳过氧化物酶活性的影响也不尽相同,Fe3+对酶的抑制作用明显,而Mg2+对酶反应有一定的激活作用。
Soybean Hull Peroxidase（SHP）,isolated from soybean hull,is a kind of important oxidoreductase.We extract SHP with buffer solution to determine the enzymatic activity with guaiacol method.The results show that SHP is high-temperature resisted and acid-alkai resisted,and the optimum temperature for SHP is 35 ℃,the optimum pH is 5.2,Km values of guaiacol and peroxide are 1.53 mmol/L and 0.36 mmol/L respectively.The effects of common compounds on SHP activity is totally different,for instance,Fe3＋ strongly inhibition influence on SHP activity,while Mg2＋ can improve the activity of SHP.
出处
《长春工业大学学报》
CAS
2010年第5期506-510,共5页
Journal of Changchun University of Technology
基金
长春工业大学科学研究发展基金资助项目(2008A15)
关键词
豆壳
过氧化物酶
酶学性质
soybean hull
peroxidase
enzymatic property
