Abstract
Objective: The aim of the present study was to purify and determine the molecular weight of keratinase isolated from Streptomyces malaysiensis.Methods: For that purpose purification was done using ammonium sulphate and Sephadex-LH 100 column chromatography. Further, the fractions were pooled and subjected to molecular weight determination using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE).Results: The obtained results showed keratinase with 47.57% recovery, 3.5-fold purification and an estimated molecular mass of 27,000 Da. Keratinase showed an optimal activity at 60 οC and pH 8. Keratinase activity of the purified product was assayed with feather powder as a substrate. The isolated strain was identified as Streptomyces malaysiensis based on phylogenetic tree analysis. The strain isolated from termite mound soil showed the highest keratinase activity, which could be considered a microorganism of environmental origin.Conclusion: The production of keratinase on simple media with feathers as sole source allowing its production from the cheap substrate and a commercial production with low production cost. Stability in the presence of detergents, surfactants and solvents make this keratinase extremely useful for a biotechnological process involving keratin.
Highlights
Microbial keratinases have become biotechnologically important since they target the hydrolysis of highly rigid, strongly cross-linked structural polypeptide “keratin”
We report an efficient method for the purification and molecular weight determination of keratinase from Streptomyces malaysiensis
We describe our keratinolytic S. malaysiensis (TMS1a) able to degrade chicken feather using keratin as substrate
Summary
Microbial keratinases have become biotechnologically important since they target the hydrolysis of highly rigid, strongly cross-linked structural polypeptide “keratin”. These enzymes are largely produced in the presence of keratinous substrates in the form of hair, feather, wool, nail, horn etc. The keratinous wastes largely comprise of insoluble structural protein “keratin”. It is increasingly accumulating in the environment mainly from various industries. Today, it is becoming a part of solid waste management since it is tough to degrade due to the highly rigid structure rendered by extensive disulphide bonds and cross-linkage. There is a demand for developing biotechnological alternatives for recycling of such wastes
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