Abstract
A unique standard starch casein medium has been implemented for the isolation of actinobacteria from the south Indian marine sediments. A combination of techniques, morphological, physiological and biochemical tests provided the evidence for the isolated actinobacteria. All the 56 isolates were inoculated on milk agar and soya meal agar plates for the primary proteolytic screening and the proportional study was made by ANOVA. Among the 56 isolates, nine showed proteolytic activity in terms of making clear zone around their colony on the plates. Then, nine isolates were subjected to the secondary screening on feather broth where three isolates (IS -1, 2 and 18) showed degradation of feather between seven and ten days. The keratinolytic characters of crude enzymes were scrutinized by feather keratin as substrate and the protein concentration was determined. Then, the isolates were identified at molecular level by 16S rRNA gene amplification technique. Key words: Actinobacteria, keratinase, milk agar, soya meal agar, 16S rRNA gene amplification.
Highlights
Keratin is an insoluble protein which is resistant to degradation by peptidases, such as trypsin, pepsin and papain (Riffel et al, 2007; Zaghloal et al, 2011)
Secondary screening was done to find out the feather degrading actinobacteria among the positive isolates and IS-1, IS-2, 8 and 18 were able to degrade the feather among the nine isolates selected through primary screening
Sums of 56 actinobacteria were isolated from South Indian Coastal Region
Summary
Keratin is an insoluble protein which is resistant to degradation by peptidases, such as trypsin, pepsin and papain (Riffel et al, 2007; Zaghloal et al, 2011). The protein chains are packed tightly either in α- helix (αKeratin) or in β- sheet (β- Keratins) structures which fold into final 3-dimensional form (Kim, 2007). Keratin forms a major component of the epidermis and its appendages via hair, feather, nails, horns, hoofs, scales and wool. Keratins are grouped into hard and soft keratins according to the sulfur content. Hard keratins are found in appendages; whereas, soft keratins like skin and callus have low content of disulphide bond (Scrooyen et al, 2001). Keratinases [EC 3.4.21/24/99.11] are large serine or metallo proteases capable of degrading the structure forming keratinous proteins (Ramani et al, 2005). The applications are feather elimination, biodegradable films, glues and foils, cosmetics, leather industry and nitrogenous fertilizer for plants (Detoni et al, 2002; Gousteroa et al, 2005)
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