Dataset Information

Sulfitolytic and keratinolytic potential of Chryseobacterium sp. RBT revealed hydrolysis of melanin containing feathers.

ABSTRACT: In black feathers, melanin is embedded in keratin matrix that makes feather more resistance to the microbial degradation. Chryseobacterium sp. RBT previously isolated from the poultry waste disposable site revealed strong sulfitolytic and keratinolytic activities. Maximum keratinase activity was observed at 48 h (89.12 U ml-1) showed 83 % of native black feather degradation. The concentration of free sulfhydryl groups released during degradation was 0.648 × 10-4 M (12 h), 2.144 × 10-4 M (96 h), and however, declined on prolong incubation to 1.752 × 10-4 M (120 h). Melanin was released in the degradation medium after microbial exploitation of black feather. After purification, melanin was dark brown colored powder insoluble in water, 5 M HCL, ethanol, methanol, benzene, chloroform, and acetone; whereas, soluble in KOH and NaOH. On exposure to oxidizing and reducing reagents feather melanin showed decolorization, while formed a brown precipitate when reacted with FeCl3. The spectroscopic characterization of isolated melanin demonstrated absorption at infra-red region. Similarly, UV-visible scan confirmed that increase in the wavelength progressively declined the absorbance of pigment. The crude keratinase enzyme (2 % v/v) produced during degradation showed complete dehairing of goat skin within 20 h.

SUBMITTER: Gurav RG

PROVIDER: S-EPMC4919140 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Sulfitolytic and keratinolytic potential of Chryseobacterium sp. RBT revealed hydrolysis of melanin containing feathers.

Gurav Ranjit G RG Tang Jingchun J Jadhav Jyoti P JP

3 Biotech 20160623 2

In black feathers, melanin is embedded in keratin matrix that makes feather more resistance to the microbial degradation. Chryseobacterium sp. RBT previously isolated from the poultry waste disposable site revealed strong sulfitolytic and keratinolytic activities. Maximum keratinase activity was observed at 48 h (89.12 U ml<sup>-1</sup>) showed 83 % of native black feather degradation. The concentration of free sulfhydryl groups released during degradation was 0.648 × 10<sup>-4</sup> M (12 h), 2 ...[more]

PMID: 28330217

Similar Datasets

Project description:Microbial keratinases' versatility in the beneficiation of keratinous waste biomass into high-value products prompts their application in diverse spheres hence, advancing green technology and the bioeconomy. Consequently, a feather-degrading Chryseobacterium aquifrigidense FANN1 (NCBI: MW169027) was used to produce keratinase, and its biochemical properties were determined. The optimization of physicochemical parameters and analysis of the free amino acid constituents of the feather hydrolysate were also carried out. FANN1 showed a maximum keratinase yield of 1,664.55 ± 42.43 U/mL after 72 h, at optimal process conditions that included initial medium pH, incubation temperature, inoculum size, and chicken feather concentration of 8, 30°C, 4% (v/v), and 15 (g/L), respectively. Analysis of degradation product showed 50.32% and 23.25% as the protein value and total free amino acids, respectively, with a relatively high abundance of arginine (2.25%) and serine (2.03%). FANN1 keratinase was optimally active at pH 8.0 and relatively moderate to high temperature (40-50°C). EDTA and 1,10-phenanthroline inhibited the keratinase activity, and that suggests a metallo-keratinase. The enzyme showed remarkable stability in the presence of chemical agents, with residual activity 141 ± 10.38%, 98 ± 0.43%, 111 ± 1.73%, 124 ± 0.87%, 104 ± 3.89%, 107 ± 7.79%, and 112 ± 0.86% against DTT, H2O2, DMSO, acetonitrile, triton X-100, tween-80, and SDS, respectively. The residual activity of FANN1 keratinase was enhanced by Sunlight (129%), Ariel (116%), MAQ (151%), and Surf (143%) compared to the control after 60 min preincubation. Likewise, the enzyme was remarkably stable in the presence Fe3+ (120 ± 5.06%), Ca2+ (100 ± 10.33%), Na+ (122 ± 2.95%), Al3+ (106 ± 10.33%); while Co2+ (68 ± 8.22%) and Fe2+ (51 ± 8.43%) elicited the most repressive effect on keratinase activity. The findings suggest that C. aquifrigidense FANN1 is a potential candidate for keratinous wastes bio-recycling, and the associated keratinase has a good prospect for application in detergent formulation.

Dataset Information

Sulfitolytic and keratinolytic potential of Chryseobacterium sp. RBT revealed hydrolysis of melanin containing feathers.

Publications

Sulfitolytic and keratinolytic potential of Chryseobacterium sp. RBT revealed hydrolysis of melanin containing feathers.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets