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Keratinolytic proteases of Bacillus species isolated from the Amazon basin showing remarkable de-hairing activity
Three keratinolytic Bacillus spp. isolated from the Brazilian Amazon basin were characterized. The strains P6, P7 and P11 were identified based on morphological and biochemical characteristics and 16S rDNA sequences. P6, P7 and P11 sequences shared more than 99% similarity with B. subtilis, B. amylo...
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Published in: | World journal of microbiology & biotechnology 2007-03, Vol.23 (3), p.375-382 |
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creator | Giongo, Janice Luhering Lucas, Françoise S Casarin, Franciani Heeb, Philipp Brandelli, Adriano |
description | Three keratinolytic Bacillus spp. isolated from the Brazilian Amazon basin were characterized. The strains P6, P7 and P11 were identified based on morphological and biochemical characteristics and 16S rDNA sequences. P6, P7 and P11 sequences shared more than 99% similarity with B. subtilis, B. amyloliquefaciens and B. velesensis. The keratinases produced by these bacteria were active on azokeratin and degradation of feather barbules was observed. The enzymes were inhibited by the serine protease inhibitor PMSF, and showed maximum activity at pH 9.0. Proteins like albumin, casein and gelatin were hydrolysed by these keratinases. Depilatory studies on bovine pelts revealed that all three strains were efficient in promoting de-hairing. Microscopic analysis showed that the epidermis was completely removed and the absence of hair in follicles was observed. |
doi_str_mv | 10.1007/s11274-006-9234-1 |
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The strains P6, P7 and P11 were identified based on morphological and biochemical characteristics and 16S rDNA sequences. P6, P7 and P11 sequences shared more than 99% similarity with B. subtilis, B. amyloliquefaciens and B. velesensis. The keratinases produced by these bacteria were active on azokeratin and degradation of feather barbules was observed. The enzymes were inhibited by the serine protease inhibitor PMSF, and showed maximum activity at pH 9.0. Proteins like albumin, casein and gelatin were hydrolysed by these keratinases. Depilatory studies on bovine pelts revealed that all three strains were efficient in promoting de-hairing. Microscopic analysis showed that the epidermis was completely removed and the absence of hair in follicles was observed.</description><identifier>ISSN: 0959-3993</identifier><identifier>EISSN: 1573-0972</identifier><identifier>DOI: 10.1007/s11274-006-9234-1</identifier><language>eng</language><publisher>Dordrecht: Dordrecht : Kluwer Academic Publishers</publisher><subject>Bacillus ; Bacillus (bacteria) ; Bacteria ; Biochemistry ; Biodiversity ; Biological and medical sciences ; Biotechnology ; Depilatory activity ; Ecology, environment ; Epidermis ; feathers ; Fundamental and applied biological sciences. 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The strains P6, P7 and P11 were identified based on morphological and biochemical characteristics and 16S rDNA sequences. P6, P7 and P11 sequences shared more than 99% similarity with B. subtilis, B. amyloliquefaciens and B. velesensis. The keratinases produced by these bacteria were active on azokeratin and degradation of feather barbules was observed. The enzymes were inhibited by the serine protease inhibitor PMSF, and showed maximum activity at pH 9.0. Proteins like albumin, casein and gelatin were hydrolysed by these keratinases. Depilatory studies on bovine pelts revealed that all three strains were efficient in promoting de-hairing. Microscopic analysis showed that the epidermis was completely removed and the absence of hair in follicles was observed.</description><subject>Bacillus</subject><subject>Bacillus (bacteria)</subject><subject>Bacteria</subject><subject>Biochemistry</subject><subject>Biodiversity</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Depilatory activity</subject><subject>Ecology, environment</subject><subject>Epidermis</subject><subject>feathers</subject><subject>Fundamental and applied biological sciences. 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The strains P6, P7 and P11 were identified based on morphological and biochemical characteristics and 16S rDNA sequences. P6, P7 and P11 sequences shared more than 99% similarity with B. subtilis, B. amyloliquefaciens and B. velesensis. The keratinases produced by these bacteria were active on azokeratin and degradation of feather barbules was observed. The enzymes were inhibited by the serine protease inhibitor PMSF, and showed maximum activity at pH 9.0. Proteins like albumin, casein and gelatin were hydrolysed by these keratinases. Depilatory studies on bovine pelts revealed that all three strains were efficient in promoting de-hairing. 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subjects | Bacillus Bacillus (bacteria) Bacteria Biochemistry Biodiversity Biological and medical sciences Biotechnology Depilatory activity Ecology, environment Epidermis feathers Fundamental and applied biological sciences. Psychology Keratinase leather Life Sciences Microbiology Microscopic analysis Protease Proteinase inhibitors |
title | Keratinolytic proteases of Bacillus species isolated from the Amazon basin showing remarkable de-hairing activity |
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