Degradation of keratin and collagen containing wastes by newly isolated thermoactinomycetes or by alkaline hydrolysis

Gousterova, A.; Braikova, D.; Goshev, Ivan; Christov, Plamen P.; Tishinov, Kiril; Vasileva−Tonkova, Evgenia; Haertlé, Thomas; Nedkov, P.

doi:10.1111/j.1472-765x.2005.01692.x

Cited by 135 publications

(85 citation statements)

References 21 publications

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“…keratin) in an autoclave [29] or by microwaves [30]. In this study, this method has been applied to hydrolyze collagen and other organic compounds using an autoclave.…”

Section: Introductionmentioning

confidence: 99%

Physiochemical characterizations of hydroxyapatite extracted from bovine bones by three different methods: Extraction of biologically desirable HAp

Barakat

Khalil

Sheikh

et al. 2008

Materials Science and Engineering: C

168

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“…keratin) in an autoclave [29] or by microwaves [30]. In this study, this method has been applied to hydrolyze collagen and other organic compounds using an autoclave.…”

Section: Introductionmentioning

confidence: 99%

Physiochemical characterizations of hydroxyapatite extracted from bovine bones by three different methods: Extraction of biologically desirable HAp

Barakat

Khalil

Sheikh

et al. 2008

Materials Science and Engineering: C

168

View full text Add to dashboard Cite

“…Owing to their insoluble nature, feathers are resistant to degradation by common microbial proteases. Thus, the several million tons of feathers generated annually by the poultry industry leads to troublesome environmental pollution and wastage of protein-rich reserve (Onifade et al, 1998;Gousterova et al, 2005;Grazziotin et al, 2006). Keratinase enzymes have been found to be an effective feather degrading enzyme useful for degradation of feather, hair and chicken wastes.…”

Section: Discussionmentioning

confidence: 99%

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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“…The non-conventional sources like wastes from agriculture, poultry, meat and fish industry have been exploited to meet the demand of lowcost protein foods. Studies have shown that keratin hydrolysates may serve as good organic fertilizers (Gousterova et al 2005) and as amino acid supplements for health foods and pet foods (Gupta and Ramnani 2006). Two keratinases produced by B. licheniformis PWD-1, i.e.…”

Section: Proteases For Processing Of Keratin Wastesmentioning

confidence: 99%

Potential application spectrum of microbial proteases for clean and green industrial production

Singh

Bajaj

2017

Energ. Ecol. Environ.

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Enzymes are the cornerstones of metabolism and constitute the fundamental basis for existence of life. However, recently enzymes are being implicated in diverse industrial processes because of their specific and fast action for efficient bioconversion of substrate to product, and their capability to save raw materials, energy and chemicals for various manufacturing processes. Enzymes are considered as environment-friendly (green) chemicals that may potentially help replacing completely or reducing the usage of hazardous chemicals for industrial processes, thus promising sustainable production and manufacturing. Among various industrial enzymes microbial proteases dominate the world enzyme market due to their multifaceted application potential in varied bioindustries like food, pharmaceutical, textile, photographic, leather and detergent. Promising applications of proteases in agricultural sector for instance may include biocontrol of pests, degumming of silk, selective delignification of hemp and wool processing. However, for successful industrial applications the proteases must be robust enough to suit the process conditions which are generally hostile. Proteases intended for industrial applications must have activity and stability over wide range of temperature and pH extremes for prolonged time periods and even in the presence of various potential enzyme inhibitors. Of various microbial proteases those from Bacillus spp. have got special significance because the latter are known for their ability to produce sturdy enzymes that might have suitability for industrial process conditions. The current article presents an interpretive summary of the recent developments on application potential of proteases for various industries.

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Degradation of keratin and collagen containing wastes by newly isolated thermoactinomycetes or by alkaline hydrolysis

Cited by 135 publications

References 21 publications

Physiochemical characterizations of hydroxyapatite extracted from bovine bones by three different methods: Extraction of biologically desirable HAp

Physiochemical characterizations of hydroxyapatite extracted from bovine bones by three different methods: Extraction of biologically desirable HAp

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

Potential application spectrum of microbial proteases for clean and green industrial production

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