首页> 外文期刊>Journal of Microbiology, Biotechnology and Food Sciences >THERMOPHILIC BACILLUS LICHENIFORMIS RBS 5 ISOLATED FROM HOT TUNISIAN SPRING CO-PRODUCING ALKALINE AND THERMOSTABLE α-AMYLASE AND PROTEASE ENZYMES
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THERMOPHILIC BACILLUS LICHENIFORMIS RBS 5 ISOLATED FROM HOT TUNISIAN SPRING CO-PRODUCING ALKALINE AND THERMOSTABLE α-AMYLASE AND PROTEASE ENZYMES

机译:从突尼斯春季热共生产碱性和热固性α-淀粉酶和蛋白酶分离的嗜热芽孢杆菌RBS 5

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Bacillus licheniformis RBS 5 was isolated from thermal spring in Tunisia. The isolate coproduce α-amylase and protease enzymes. The α-amylase activity showed an optimal activity at approximately 65°C and in wide pH interval ranging from 4 to 9. This enzyme was stable over the range of 45 to 70°C after 30 min of incubation and in the pH range of 8 to 10. Protease activity was optimal; at 80°C, pH 12. This enzyme was stable until 60°C over the pH range of 10 to 12. EDTA at concentration of 5 mM reduces slightly both activities evoking the serine alkaline protease. Cationic ions (Ca2+, Cu2+, Zn2+, and Mg 2+) have an inhibition effect on α-amylase. However, protease activity was enhanced by Ca2+, Cu2+ and Mg 2+); the other cations reduce slightly the proteolytic activity. SDS and H2O2 were found as inhibitors for both activities whereas Triton X-100 and perfume have no effect. Taken together, these traits make protease activity of B. licheniformis RBS 5 as efficient for use in detergent industry.
机译:地衣芽孢杆菌RBS 5是从突尼斯温泉中分离出来的。分离物共同产生α-淀粉酶和蛋白酶。 α-淀粉酶的活性在约65°C和4至9的宽pH区间内显示出最佳活性。孵育30分钟后,在8至pH范围内,该酶在45至70°C的范围内稳定。至10。蛋白酶活性最佳;在80°C,pH 12下,该酶在10至12的pH范围内一直稳定到60°C。浓度为5 mM的EDTA略微降低了丝氨酸碱性蛋白酶的两种活性。阳离子(Ca2 +,Cu2 +,Zn2 +和Mg 2+)对α-淀粉酶具有抑制作用。然而,Ca2 +,Cu2 +和Mg 2+增强了蛋白酶的活性。其他阳离子则稍微降低蛋白水解活性。 SDS和H2O2被发现是两种活性的抑制剂,而Triton X-100和香料没有作用。综上所述,这些特性使地衣芽孢杆菌RBS 5的蛋白酶活性有效用于洗涤剂工业。

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