Purification and Characterization of Keratinase fromFeather Degrading Bacillus sp.

The Internet journal of microbiology Pub Date : 2009-12-31 DOI:10.5580/159b

Jeevana Lakshmi. Peddu, C. Chitturi, V. Lakshmi

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引用次数: 4

Abstract

Microorganisms producing keratinases are gaining prominence in recycling of poultry waste feather. Keratinase producing Bacillus sp. Isolated, were subjected to strain improvement along with optimisation of parameters of fermentation. Scaled up enzyme was partially purified and characterized to evaluate its application potential. Keratinase isolated from the bacillus species exhibited good stability with > 90% activity being retained for one month at refrigerated conditions and 50% activity was observed even after two months. At room temperature, the enzyme was active for 24 � 48 hours with optimum temperature of activity being 55∞C. The activity range was between 28∞C - 55∞C and pH optima was 8.5 which matched with optima for production of the enzyme. ~38kDa keratinase produced by the isolates was categorized into subtilisin group of serine proteinase based on the sensitivity to protease inhibitors, Keratinase from the test isolates was only marginally affected by surfactants, organic solvents. A significant enhancement in activity was observed in presence of reducing agents indicating possible versatile application potential for this enzyme with high stability

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羽毛降解芽孢杆菌中角化酶的纯化及特性研究。

产生角化酶的微生物在家禽废羽毛的回收利用中日益突出。对分离得到的产角蛋白酶芽孢杆菌进行菌种改良，并对发酵条件进行优化。对放大酶进行了部分纯化和表征，以评价其应用潜力。从芽孢杆菌中分离出的角蛋白酶表现出良好的稳定性，在冷藏条件下保持一个月的活性大于90%，即使在两个月后也保持50%的活性。室温条件下，酶活性为24 ~ 48 h，最适活性温度为55∞C。酶活范围为28∞C ~ 55∞C, pH最优值为8.5，符合酶的最优产酶条件。根据对蛋白酶抑制剂的敏感性，分离株产生的~38kDa角化酶可归为丝氨酸蛋白酶枯草菌素组，表面活性剂、有机溶剂对分离株角化酶的影响较小。在还原剂的存在下，酶的活性显著增强，表明该酶具有高稳定性，具有广泛的应用潜力

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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The Internet journal of microbiology

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