Hide Dehairing and Laundry Detergent Compatibility Testing of Thermostable and Solvents Tolerant Alkaline Protease from Hot Spring Isolate &lt;i&gt;Bacillus cohnii&lt;/i&gt;U3

Bhavsar Sunil,Ghelani Anjana,Pravin R Dudhgara

doi:10.3844/ojbsci.2015.152.161

Abstract

In the present study, alkaline protease producing thermophilic Bacillus cohniiU3 strain was isolation from Unnai hot spring, India. The maximum production of protease (344 U/mL) was reported after 72 h of inoculation at 50°C in shake flask culture using the gelatin casein medium. The protease was found to remain active up to 96 h and production was growth dependent. The activity of parital purified protease was reported 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. Salt independent catalysis and activity with a broad range of substrate concentration is the key feature of the protease. Thermos table nature, the stability in alkaline pH and stability in high salt concentration for 45 min were outstanding features of protease. The enzyme was stable in the presence of various organic solvents like Dimethyl Sulphoxide (DMSO), Methanol, Butanol, n-Hexane, Benzene at 25% (v/v) concentration. A good compatibility of the enzyme with most commercial detergents indicated its application in detergent industry. The remarkable dehairing in goat hide and destaining of blood spot in 2 h using 10 U/mL of protease assure that it could be a potential candidate for leather and detergent industries.

Highlights

With an increasing emphasis on environmental protection, the use of hydrolytic enzymes from thermophiles, has gained significant attention in many industrial processes
Isolation of strain was carried out by the enrichment of water collected from Unnai hot spring (20°85′33′′N, 73°33′42′′E), India into Gelatin Casein (GC) broth containing g/L: gelatin, 5.0; casein enzymatic hydrolysate, 1.0; peptone, 5.0; yeast extract, 1.5; meat extract, 1.5; NaCl, 5.0; pH 7.5 followed by incubation at 50°C for 48 h under shake flask conditions
Isolate was identified as a moderate thermophilic Bacillus cohnii by 16s rRNA sequence analysis

Summary

Introduction

With an increasing emphasis on environmental protection, the use of hydrolytic enzymes from thermophiles, has gained significant attention in many industrial processes. Enzymes from thermophiles are of particular interest since the high temperature does not usually denature them and remain active at elevated temperature (Adams and Kelly, 1998). They are more resistant to chemical reagents and extreme pH in comparison to their mesophilic homologues (Hough and Denson, 1999). Their thermostability is associated with performing the enzymatic reaction at high temperature allows higher substrate concentrations, lower viscosity, the fewer risk of contamination and often higher reaction rates (Seatovic et al, 2004). Global requirements of thermostable biocatalysts are far greater than those of the mesophilic biocatalysts suggesting the huge need of thermophilic enzymes (Haki and Rakshit, 2003)

Methods

Discussion

Conclusion