Abstract
Earth has innate background for fungi that cover individual kingdom since evolution. The keratinophilic fungi are allied moulds that produce the keratinase enzyme to degrade the keratinous materials in or on the soil. Keratinous materials are insoluble and resistant to degradation by common proteinase enzymes. It is important to study the microorganism producers of such enzymes for use in the biotechnology industry. In order to present study, two isolates of fungi were evaluated to determine if they had the ability to degrade keratin as nutrient substrate. They were grown in an inundated culture medium containing poultry feathers. Among species, best keratin substrate degradation activity as well as keratinase enzyme activity was recorded in Arthoderma multifidium (KU578107) followed by Chrysosporium tropicum (KU578108) gradually leading manner day by days.
Highlights
In poultry processing industry with market demand of contemptible meat, the feathers wastes are gradually increasing day by day
Microscopic and molecular identification, these fungal species were identified as Arthoderma multifidium (KU578107) and Chrysosporium tropicum (KU578108)
Among the keratinophilic fungal species, best keratin substrate degradation activity was recorded in Arthoderma multifidium followed by Chrysosporium tropicum
Summary
In poultry processing industry with market demand of contemptible meat, the feathers wastes are gradually increasing day by day. The feather constitutes by βkeratin, a fibrous protein that highly cross-linked with disulfide bonds and appeared initial in 3-dimensional folds (Brandelli et al, 2010; Sharma et al, 2015a) These keratin wastes can be proficiently degraded by precise proteases such as keratinase. Keratinase is proteases which able to degrade the scleroprotein keratin that is produced by a domain of saprophytic and dermatophytes fungi, actinomycetes and other microbial species (Selvam and Vishnupriya, 2012; Sharma et al, 2015b) These groups contain a complex group of hydrolytic enzymes that disgrace to proteins into small amino acids. These hydrolytic enzymes attack on the carbonyl carbon of the scissile bond where the peptide bonds are cleaved by catalysis in addition of water (Bhat, 2000; Kumawat et al, 2013). This present study was aimed to evaluate the degradation of keratin from feather degradation medium and to estimate a potential use of keratinase from keratinocytes fungi origin for the industrial treatment of keratin containing materials
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