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1.
Braz. j. microbiol ; 46(3): 691-700, July-Sept. 2015. tab, ilus
Article in English | LILACS | ID: lil-755810

ABSTRACT

Keratinolytic microorganisms have become the subject of scientific interest due to their ability to biosynthesize specific keratinases and their prospective application in keratinic waste management. Among several bacterial classes, actinobacteria remain one of the most important sources of keratin-degrading strains, however members of the Micrococcaceae family are rarely scrutinized in regard to their applicatory keratinolytic potential. The tested Micrococcus sp. B1pz isolate from poultry feather waste was identified as M. luteus. The strain, grown in the medium with 1–2% chicken feathers and a yeast extract supplement, produced keratinases of 32 KU and lower level of proteases, 6 PU. It was capable to effectively decompose feathers or “soft” keratin of stratum corneum, in contrast to other “hard” hair-type keratins. The produced keratinolytic enzymes were mainly a combination of alkaline serine or thiol proteases, active at the optimum pH 9.4, 55 °C. Four main protease fractions of 62, 185, 139 and 229 kDa were identified in the crude culture fluid. The research on the auxiliary role of reducing factors revealed that reducing sulfur compounds could be applied in keratinolysis enhancement during enzymatic digestion of keratin, rather than in culture conditions. The presented M. luteus isolate exhibits a significant keratinolytic potential, which determines its feasible applicatory capacity towards biodegradation of poultry by-products or formulation of keratin-based feed components.

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Subject(s)
Animals , Keratins/metabolism , Micrococcus luteus/enzymology , Micrococcus luteus/metabolism , Peptide Hydrolases/metabolism , Biodegradation, Environmental , Chickens/microbiology , Feathers/microbiology , Micrococcus luteus/isolation & purification , NADH, NADPH Oxidoreductases/metabolism , Oxidation-Reduction , Poultry/microbiology , Sulfur Compounds/metabolism , Waste Management
2.
Indian J Biochem Biophys ; 2006 Aug; 43(4): 211-6
Article in English | IMSEAR | ID: sea-28873

ABSTRACT

High throughput macromolecular structure determination is very essential in structural genomics as the available number of sequence information far exceeds the number of available 3D structures. ACORN, a freely available resource in the CCP4 suite of programs is a comprehensive and efficient program for phasing in the determination of protein structures, when atomic resolution data are available. ACORN with the automatic model-building program ARP/wARP and refinement program REFMAC is a suitable combination for the high throughput structural genomics. ACORN can also be run with secondary structural elements like helices and sheets as inputs with high resolution data. In situations, where ACORN phasing is not sufficient for building the protein model, the fragments (incomplete model/dummy atoms) can again be used as a starting input. Iterative ACORN is proved to work efficiently in the subsequent model building stages in congerin (PDB-ID: lis3) and catalase (PDB-ID: 1gwe) for which models are available.


Subject(s)
Animals , Automation , Catalase/chemistry , Computational Biology/instrumentation , Crystallography, X-Ray , Eels , Galectins/chemistry , Genomics/methods , Micrococcus luteus/metabolism , Models, Chemical , Models, Molecular , Protein Conformation , Proteins/chemistry , Proteomics/methods , Software
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