Characterization of a new keratinolytic bacterium that completely degrades native feather keratin

Riffel, Alessandro; Lucas, Françoise; Heeb, Philipp; Brandelli, Adriano

doi:10.1007/s00203-003-0525-8

Cited by 250 publications

(226 citation statements)

References 38 publications

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“…kr6 was kept in feather meal agar plates (Riffel et al 2003). For protease production, this strain was inoculated in feather meal broth containing the following components (g L −1 ): NaCl (0.5), KH 2 PO 4 (0.4), CaCl 2 (0.015) and feather meal (10.0).…”

Section: Microorganism and Cultivation Conditionsmentioning

confidence: 99%

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

et al. 2014

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Soybean proteins are widely used as nutritional and functional food ingredients. This investigation evaluated through a 2 3 central composite design the effect of three variables (pH, temperature and enzyme/substrate (E/S) ratio) on the production of soy protein isolate (SPI) hydrolysates with a microbial protease. Soluble peptides, antioxidant activity, and foaming and emulsifying capabilities of the hydrolysates were analyzed. All variables, as well as their interactions, were significant for the soluble peptides content of SPI hydrolysates. Optimal conditions for obtaining soluble peptides were around 30-35°C, pH 6.5-9.5, and E/S ratios of 1,650-6,300 U g −1 . SPI hydrolysates produced at 30-45°C, pH 8.0-9.5, and E/S ratios of 4,000-8,000 U g −1 showed higher capacity to scavenge the 2,2′-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) radical. Models for soluble peptides and ABTS activity of hydrolysates were obtained. In the range studied, the variables had not significant influence on the ability of hydrolysates to scavenge the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical. SPI hydrolysates also presented reducing power and ability to chelate iron. Hydrolysis temperature was significant for the Fe 2+ -chelating ability of hydrolysates. Temperature of hydrolysis was significant for the foaming capacity of hydrolysates, with higher values observed at 45°C and 8,000 U g −1 . For emulsifying capacity, only E/S ratio presented a significant effect. Temperature and E/S ratio appeared to be more significant variables influencing the properties of the SPI hydrolysates. The results of this study indicate that specific hydrolysis conditions should be selected to obtain SPI hydrolysates with preferred characteristics.

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Section: Microorganism and Cultivation Conditionsmentioning

confidence: 99%

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

et al. 2014

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“…(Sangali and Brandelli, 2000) Chryseobacterium sp. (Riffel et al, 2003) Xanthomonas sp. (De-Toni et al, 2002) and Burkholderia, Chryseobacterium, Pseudomonas (Riffel and Brandell, 2006).…”

Section: Discussionmentioning

confidence: 99%

“…Bacterial keratinases are of particular interest because of their action on the degradation of the insoluble keratin substrates and generally on a broad range of protein substrates (Lin et al, 1996). Many studies monitored the production of keratinase by Bacillus licheniformis PWD-1, Fervidobacterium, Chryseobacterium sp., Streptomyces, (Sangali and Brandelli, 2000;Langeveld et al, 2003;Riffel et al, 2003). Chryseobacterium sp., strain kr6 was isolated from waste of a poultry industry and was capable to completely degrade chicken feathers.…”

Section: Introductionmentioning

confidence: 99%

“…Chryseobacterium sp., strain kr6 was isolated from waste of a poultry industry and was capable to completely degrade chicken feathers. Its extracellular keratinase is a metalloprotease with great potential for biotechnological applications (Riffel et al, 2003). Another work describes the effect of temperature, initial pH and substrates on keratinase production by Chryseobacterium sp., kr6 during growth on native feathers (Brandelli and Riffel, 2005).…”

Section: Introductionmentioning

confidence: 99%

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Biochemical and Molecular Characterization of a New Local Keratinase Producing Pseudomomanas sp., MS21

Tork¹,

Aly²,

Nawar³

2009

Asian J. of Biotechnology

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This study aimed to isolate and identify a new local bacterial strain, able to completely degrade keratin-rich wastes into soluble and useful materials which can be used in many proposes. Bacterial keratinases are of particular interest because of their action on insoluble keratin substrates and generally on a broad range of protein substrates. These enzymes have been studied for de-hairing processes in the leather industry and hydrolysis of feather and keratin. Samples from poultry industry wastes, soil, water, fodder and feather were collected from different places in Jeddah, Saudi Arabia. Each sample was plated on feather meal agar plates containing 5 g LG feather as the sole carbon and nitrogen source and 1 the obtained colonies were selected, purified and their growth were detected on skimmed milk agar and feather meal broth media. The well grown isolates on feather meal agar which producing the largest clearing zone on skimmed milk plate were selected for keratinase assays. Out of 23 bacterial isolates, 7 isolates were selected. The best keratinase producing bacterium kera MS21 was selected and identified based on morphological, physiological and some biochemical characteristics. It was recorded as a species belonging to the genus Pseudomonas and identified as Pseudomonas sp. The results of identification were confirmed by 16S rDNA studies. Precipitation and purification of the keratinase enzyme in addition to factors affecting enzyme activity were studied. The enzyme molecular weight was determined to be of 30 KDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. The optimum temperature and pH were determined to be 37°C and pH 8.0, respectively. The effect of some proteases inhibitors and activators were also studied.

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“…Riffel et al (2003) determined the residual activities of bacterial enzymes after incubation with organic solvents, the remaining activities being between 56 and 70%. Enzyme D was completely inhibited when incubated with calcium carbonate.…”

Section: Inhibitors Of Enzymes Activitiesmentioning

confidence: 99%

Hide unhairing and characterization of commercial enzymes used in leather manufacture

Dettmer

Ayub

Gutterres

2011

Braz. J. Chem. Eng.

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-The enzymatic treatment of hides in tannery processes is a promising technology. However, the reaction kinetics of commercial enzymes available to the leather industry are not fully understood and their activities have been mainly determined with model proteins such as casein as substrate, which are not of direct relevance for cattle hides. Therefore, it is important to determine their activities on collagen and keratin, the main proteins of skin, in order to use these enzymes in leather processing. This work describes the study of five proteases, used commercially in tanneries, to assess their ability to act upon collagen and keratin and to determine their unhairing. Results showed that all commercial enzymes tested had more activity on collagen than on keratin. Unhairing was also tested and four out of the five enzymes tested showed some unhairing activity. Optima of the temperature and pH of the enzymes were very similar for all five enzymes, with maximal activities around 55°C and pH 9 to 12, respectively.

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Characterization of a new keratinolytic bacterium that completely degrades native feather keratin

Cited by 250 publications

References 38 publications

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

Biochemical and Molecular Characterization of a New Local Keratinase Producing Pseudomomanas sp., MS21

Hide unhairing and characterization of commercial enzymes used in leather manufacture

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