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Anissa Haddar,Noomen Hmidet,Olfa Ghorbel-Bellaaj,Nahed Fakhfakh-Zouari,Alya Sellami-Kamoun,Moncef Nasri 한국생물공학회 2011 Biotechnology and Bioprocess Engineering Vol.16 No.4
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°C and at an enzyme/substrate (E/S) 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°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.
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Rayda Siala,Nahed Fakhfakh,Ibtissem Hamza-Mnif,Moncef Nasri,Tatiana Vallaeys,Alya Sellami-Kamoun 한국생물공학회 2012 Biotechnology and Bioprocess Engineering Vol.17 No.3
Arthrobacter arilaitensis Re117 protease described here is the first Arthrobacter alkaline metalloprotease studied. It was purified to homogeneity by Sephadex G-100 gel filtration, ultrafiltration, and Mono Q-Sepharose with 3.72-fold increase in specific activity and 28.22%recovery. The molecular mass of the purified enzyme was estimated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) at 50 kDa. The N-terminal amino acid sequence QASTAYSQIDDF, showed high homology with Pseudomonas metalloproteases. The enzyme was highly active over a wide range of pH from 6.0 to 11.0, with an optimum activity at pH 9.0 and 40°C. The proteolytic activity was totally lost in the presence of Ethylene Diamine Tetraacetic Acid. Among the tested protein substrates, casein served as the most preferred for the enzyme, followed by fibrin. Purified metalloprotease exhibited significant stability and compatibility with nonionic surfactants (Tween 20, Tween 80, and Triton X-100),oxidizing agents (H2O2 and sodium perborate), and most of the tested commercial laundry detergents, demonstrating its feasibility for inclusion in detergent formulations.
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