Partial Purification and Characterization of Protease from Abrus precatorius Linn. (Fabaceae) from Cameroon
Partial Purification and Characterization of Protease from Abrus precatorius Linn. (Fabaceae) from Cameroon作者机构：Bioprocess Laboratory Unit of Food Sciences and nutrition University Institute of Technology University of Ngaoundere Ngaoundere Cameroon
出 版 物：《Advances in Enzyme Research》 (酶研究进展（英文）)
年 卷 期：2016年第4卷第2期
页 面：35-43页
学科分类：1008[医学-中药学(可授医学、理学学位)] 1006[医学-中西医结合] 100602[医学-中西医结合临床] 10[医学]
主 题：A. precatorius Cameroon Proteases Partial Purified Extract Proteolytic Activity
摘 要：Crude enzyme extracts were prepared from leaves and stems of Linn. (Fabaceae) from Cameroon under optimized conditions. Proteolytic enzymes were precipitated with ammonium sulfate at 35% (w/v) saturation and assayed for enzyme activity. The effects of temperature, pH, incubation time and substrate specificity were studied. SDS-PAGE was used to determine molecular weight of precipitated protease. Results indicated that proteolytic activity of crude extract was 35.20 U/ml compared to 51.03 U/ml of partial purified extract. The optimum enzyme activity was found to be at 40°C, while 50% of activity was maintained at 60°C after 60 min incubation. Partial purified crude extract exhibited two optimum pH (2.75 and 9.0). The highest enzyme activity towards Bovine Serum Albumine (25.9 U/ml) was noted. SDS-PAGE gels exhibited molecular weight between 40 - 60 KDa. This result confirms that partial purified extract of A. precatorius contains proteases and could be a promising source for proteolytic enzyme extraction.
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