Abstract

The search for novel renewable products over synthetics hallmarked this decade and those of the recent past. Most economies that are prospecting on biodiversity for improved bio-economy favor renewable resources over synthetics for the potential opportunity they hold. However, this field is still nascent as the bulk of the available resources are non-renewable based. Microbial metabolites, emphasis on secondary metabolites, are viable alternatives; nonetheless, vast microbial resources remain under-exploited; thus, the need for a continuum in the search for new products or bio-modifying existing products for novel functions through an efficient approach. Environmental distress syndrome has been identified as a factor that influences the emergence of genetic diversity in prokaryotes. Still, the process of how the change comes about is poorly understood. The emergence of new traits may present a high prospect for the industrially viable organism. Microbial enzymes have prominence in the bio-economic space, and proteases account for about sixty percent of all enzyme market. Microbial keratinases are versatile proteases which are continuously gaining momentum in biotechnology owing to their effective bio-conversion of recalcitrant keratin-rich wastes and sustainable implementation of cleaner production. Keratinase-assisted biodegradation of keratinous materials has revitalized the prospects for the utilization of cost-effective agro-industrial wastes, as readily available substrates, for the production of high-value products including amino acids and bioactive peptides. This review presented an overview of keratin structural complexity, the potential mechanism of keratin biodegradation, and the environmental impact of keratinous wastes. Equally, it discussed microbial keratinase; vis-à-vis sources, production, and functional properties with considerable emphasis on the ecological implication of microbial producers and catalytic tendency improvement strategies. Keratinase applications and prospective high-end use, including animal hide processing, detergent formulation, cosmetics, livestock feed, and organic fertilizer production, were also articulated.

Highlights

  • Keratin, a fibrous and structural polypeptide, is highly recalcitrant to degradation by common proteolytic processes due to its molecular architecture

  • Sangali and Brandelli (2000) observed that the keratinase produced by Vibrio sp. kr2 was active toward azokeratin, azocasein, benzoyl-arginine p-nitroanilide, and Alanyl-L-Alanine p-nitroanilide as substrates, and this is an indication that the keratinase produced by strain kr2 may have the potential for different industrial processes and application

  • This study presented comprehensive progress in the field of microbial keratinase research

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Summary

Introduction

A fibrous and structural polypeptide, is highly recalcitrant to degradation by common proteolytic processes due to its molecular architecture. Microbial proteolytic enzymes capable of effectively degrading keratin are referred to as keratinases (3.4.21/24/99) and are considered highly valuable in many biotechnological processes due to their robustness in management of recalcitrant substrates and appreciable stability under extreme conditions (Abdel-fattah et al, 2015).

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