Chitinases are a group of hydrolytic enzymes that catalyze chitin, nd are synthesized by a wide variety of organisms. In nature, microbial chitinases are primarily responsible for chitin decomposition. Several chitinases have been reported and characterized, and they are garnering increasing attention for their uses in a wide range of applications. In the food industry, the direct fermentation of seafood, such as crab and shrimp shells, using chitinolytic microorganisms has contributed to increased nutritional benefits through the enhancement of chitin degradation into chitooligosaccharides. These compounds have been demonstrated to improve human health through their antitumor, antimicrobial, immunomodulatory, antioxidant, and anti-inflammatory properties. Moreover, chitinase and chitinous materials are used in the food industry for other purposes, such as the production of single-cell proteins, chitooligosaccharides, N-acetyl D-glucosamines, biocontrol, functional foods, and various medicines. The functional properties and hydrolyzed products of chitinase, however, depend upon its source and physicochemical characteristics. The present review strives to clarify these perspectives and critically discusses the advances and limitations of microbial chitinase in the further production of functional foods.

Microbial chitinases: properties, current state and biotechnological applications.

Enzymatic conversion and recovery of protein, chitin, and astaxanthin from shrimp shell waste

Keratinases belong to a class of proteases that are able to degrade keratins into amino acids. Microbial keratinases play important roles in turning keratin-containing wastes into value-added products by participating in the degradation of keratin. Keratin is found in human and animal hard tissues, and its complicated structures make it resistant to degradation by common proteases. Although breaking disulfide bonds are involved in keratin degradation, keratinase is responsible for the cleavage of peptides, making it attractive in pharmaceutical and feather industries. Keratinase can serve as an important tool to convert keratin-rich wastes such as feathers from poultry industry into diverse products applicable to many fields. Despite of some progress made in isolating keratinase-producing microorganisms, structural studies of keratinases, and biochemical characterization of these enzymes, effort is still required to expand the biotechnological application of keratinase in diverse fields by identifying more keratinases, understanding the mechanism of action and constructing more active enzymes through molecular biology and protein engineering. Herein, this review covers structures, applications, biochemistry of microbial keratinases, and strategies to improve its efficiency in keratin degradation.

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Structure, Application, and Biochemistry of Microbial Keratinases.

Chitosanase (E.C. 3.2.1.132) can be used to selectively produce partially-acetylated chitosan oligosaccharides (COSs), which are functional biopolymers that can widely be utilized as environmentall...

Biocatalysis of Heterogenously-Expressed Chitosanase for the Preparation of Desirable Chitosan Oligosaccharides Applied against Phytopathogenic Fungi

Chitinases are a category of hydrolytic enzymes that catalyze chitin and are formed by a wide variety of microorganisms. In nature, microbial chitinases are primarily responsible for chitin decomposition and play a vital role in the balance of carbon and nitrogen ratio in the ecosystem. The physicochemical attributes and the source of chitinase are the main bases that determine their functional characteristics and hydrolyzed products. Several chitinases have been reported and characterized, and they obtain a wider consideration for their utilization in a large number of uses such as in agriculture, food, environment, medicine and pharmaceutical companies. The antifungal and insecticidal impacts of several chitinases have been extensively studied, aiming to protect crops from phytopathogenic fungi and insects. Chitooligosaccharides synthesized by chitin degradation have been shown to improve human health through their antimicrobial, antioxidant, anti-inflammatory and antitumor properties. This review aims at investigating chitinase production, properties and their potential applications in various biotechnological fields.

Microbial chitinases: properties, enhancement and potential applications.

Feather waste is the highest protein-containing resource in nature and is poorly reused. Bioconversion is widely accepted as a low-cost and environmentally benign process, but limited by the availability of safe and highly efficient feather degrading bacteria (FDB) for its industrial-scale fermentation. Excessive focuses on keratinase and limited knowledge of other factors have hindered complete understanding of the mechanisms employed by FDB to utilize feathers and feather cycling in the biosphere. Streptomyces sp. SCUT-3 can efficiently degrade feather to products with high amino acid content, useful as a nutrition source for animals, plants and microorganisms. Using multiple omics and other techniques, we reveal how SCUT-3 turns on its feather utilization machinery, including its colonization, reducing agent and protease secretion, peptide/amino acid importation and metabolism, oxygen consumption and iron uptake, spore formation and resuscitation, and so on. This study would shed light on the feather utilization mechanisms of FDBs.

/pdf/the-feather-degradation-mechanisms-of-a-new-streptomyces-sp-1sfkflsw6p.pdf

The feather degradation mechanisms of a new Streptomyces sp. isolate SCUT-3.

Heterologous expression and characterization of an antifungal chitinase (Chit46) from Trichoderma harzianum GIM 3.442 and its application in colloidal chitin conversion.

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The feather degradation mechanisms of a new Streptomyces sp. isolate SCUT-3.

Heterologous expression and characterization of an antifungal chitinase (Chit46) from Trichoderma harzianum GIM 3.442 and its application in colloidal chitin conversion.