Abstract

Keratinases are proteolytic enzymes predominantly active when keratin substrates are available that attack disulfide bridges in the keratin to convert them from complex to simplified forms. Keratinases are essential in preparation of animal nutrients, protein supplements, leather manufacture, textile processing, detergent formulation, feather meal processing for feed and fertilizer, the pharmaceutical and biomedical industries, and waste management. Accordingly, it is necessary to develop a method for continuous production of keratinase from reliable sources that can be easily managed. Microbial keratinase is less expensive than conventionally produced keratinase and can be obtained from fungi, bacteria, and actinomycetes. In this overview, the expansion of information about microbial keratinases and important considerations in keratinase production are discussed.

Highlights

  • Keratin is one of the most abundant biopolymers in the world [1]; it is a tough, fibrous, insoluble material that functions as an outer coat of human and animal organs, to prevent the loss of body fluids

  • Keratin is rich in sulfur compounds with disulfide bridges, which imparts them with an insoluble nature

  • We elaborated the currently available information pertaining to microbial keratinase production

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Summary

Introduction

Keratin is one of the most abundant biopolymers in the world [1]; it is a tough, fibrous, insoluble material that functions as an outer coat of human and animal organs, to prevent the loss of body fluids. The structural component of feathers, hair, nails, horns, hooves, bones, furs, claws, hides, bird beaks, skin, wool, scales, and bristle is made up of keratin (Figure 1). Α-keratins (alphahelix) are usually found in the hair, wool, horns, nails, claws, and hooves of mammals, whereas the harder β-keratin (betasheets) is found in bird feathers, beaks, and claws. Keratin is rich in sulfur compounds with disulfide bridges, which imparts them with an insoluble nature. It contains a variety of amino acids, predominantly cystine, lysine, proline, and serine. The disposal of feathers is accompanied by natural falling of feathers and hairs from birds during production, so it is necessary to develop methods to reduce keratin accumulation. We elaborated the currently available information pertaining to microbial keratinase production

Keratinophilic Fungi
Keratin-Degrading Bacterial Isolates
Secretion of Microbial Keratinases
Optimized Conditions for Microbial Keratinases
Purification of Keratinases
Acceleration of Microbial Keratinase Production
Sensing Keratinases
Findings
Perspectives
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