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Alkaline Proteases Produced by Bacillus licheniformis RP1 Grown on Shrimp Wastes: Application in Chitin Extraction, Chicken Feather-degradation and as a Dehairing Agent
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  • Alkaline Proteases Produced by Bacillus licheniformis RP1 Grown on Shrimp Wastes: Application in Chitin Extraction, Chicken Feather-degradation and as a Dehairing Agent
  • Alkaline Proteases Produced by Bacillus licheniformis RP1 Grown on Shrimp Wastes: Application in Chitin Extraction, Chicken Feather-degradation and as a Dehairing Agent
저자명
Haddar. Anissa,Hmidet. Noomen,Ghorbel-Bellaaj. Olfa,Fakhfakh-Zouari. Nahed,Sellami-Kamoun. Alya,Nasri. Moncef
간행물명
Biotechnology and bioprocess engineering
권/호정보
2011년|16권 4호|pp.669-678 (10 pages)
발행정보
한국생물공학회
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정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

The current increase in the amount of shrimp wastes produced by the shrimp industry has led to the need in finding new methods for shrimp wastes disposal. In this study, Bacillus licheniformis RP1 was shown to produce proteases when grown in media containing shrimp wastes powder as a sole carbon and nitrogen source, indicating that this bacteria could obtain its carbon and nitrogen requirements directly from shrimp wastes. The maximum protease production was obtained when the strain was grown in a medium containing (g/L): shrimp wastes powder 30, KCl 1.5, $K_2HPO_4$ 0.5, and $KH_2PO_4$ 0.5. Using casein zymography, the crude protease preparation was found to produce at least seven proteases. The proteases of B. licheniformis RP1 were tested for shrimp waste deproteinization in the preparation of chitin. The percent of protein removal after 3 h hydrolysis at $60^{circ}C$ and at an enzymestrate (ES) ratio of 0.5 and 5 (Unit of enzyme/mg of protein) were about 68 and 81%, respectively. Additionally, B. licheniformis RP1 showed important feather degrading activity. Complete solubilisation of whole feathers was observed after 24 h of incubation at $50^{circ}C$. More interestingly, the RP1 proteolytic preparation demonstrated powerful dehairing capabilities for hair removal from skin. Collagen, which is the major leather-forming protein, was not significantly degraded. Considering its promising properties, B. licheniformis RP1 enzymatic preparation may be considered a potential candidate for future use in several biotechnological processes.