期刊论文详细信息
OnLine Journal of Biological Sciences
Hide Dehairing and Laundry Detergent Compatibility Testing of Thermostable and Solvents Tolerant Alkaline Protease from Hot Spring Isolate Bacillus cohniiU3 | Science Publications
Bhavsar Sunil1  Ghelani Anjana1  Pravin R. Dudhgara1 
关键词: Alkaline Protease;    Bacillus cohnii;    Hot Spring;    Solvent Tolerant;    Detergent Compatible;    Hide Dehairing;   
DOI  :  10.3844/ojbsci.2015.152.161
学科分类:生物科学(综合)
来源: Science Publications
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【 摘 要 】

In the present study, alkalineprotease producing thermophilic Bacillus cohniiU3 strain was isolationfrom Unnai hot spring, India. The maximum production of protease (344 U/mL) wasreported after 72 h of inoculation at 50°C in shake flask culture using thegelatin casein medium. The protease was found to remain active up to 96 h andproduction was growth dependent. The activity of parital purified protease wasreported in abroad range of pH ranging from 4.0 to 11.0 with an optimum of 9.0 pH;Enzymes was indicated the highest activity at 50°C temperature. Saltindependent catalysis and activity with a broad range of substrateconcentration is the key feature of the protease. Thermos table nature, the stabilityin alkaline pH and stability in high salt concentration for 45 min wereoutstanding features of protease. The enzyme was stable in the presence ofvarious organic solvents like Dimethyl Sulphoxide (DMSO), Methanol, Butanol,n-Hexane, Benzene at 25% (v/v) concentration. A good compatibility of theenzyme with most commercial detergents indicated its application in detergentindustry. The remarkable dehairing in goat hide and destaining of blood spot in2 h using 10 U/mL of protease assure that it could be a potential candidate forleather and detergent industries.

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