Purification and partial characterization of serine-metallokeratinase from a newly isolated Bacillus pumilus NRC21

Tork, Sanaa; Shahein, Yasser E.; El-Hakim, Amr E.; Abdel‐Aty, Azza M.; Aly, Magda M.

doi:10.1016/j.ijbiomac.2016.01.060

Cited by 30 publications

(16 citation statements)

References 45 publications

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“…Except for Hg 2+ , Fe 2+ and Cu 2+ , most metal ions did not significantly affect the activity of HCLaseM. EDTA as a metal ion chelating agent hardly reduced the activity of HCLaseM, which was different from previous reports that EDTA reduced enzyme activity [24].…”

Section: Purification and Biochemical Characterization Of Hclasemcontrasting

confidence: 98%

Cloning, Expression, and Characterization of a New Glycosaminoglycan Lyase from Microbacterium sp. H14

et al. 2019

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Glycosaminoglycan (GAG) lyase is an effective tool for the structural and functional studies of glycosaminoglycans and preparation of functional oligosaccharides. A new GAG lyase from Microbacterium sp. H14 was cloned, expressed, purified, and characterized, with a molecular weight of approximately 85.9 kDa. The deduced lyase HCLaseM belonged to the polysaccharide lyase (PL) family 8. Based on the phylogenetic tree, HCLaseM could not be classified into the existing three subfamilies of this family. HCLaseM showed almost the same enzyme activity towards hyaluronan (HA), chondroitin sulfate A (CS-A), CS-B, CS-C, and CS-D, which was different from reported GAG lyases. HCLaseM exhibited the highest activities to both HA and CS-A at its optimal temperature (35 • C) and pH (pH 7.0). HCLaseM was stable in the range of pH 5.0-8.0 and temperature below 30 • C. The enzyme activity was independent of divalent metal ions and was not obviously affected by most metal ions. HCLaseM is an endo-type enzyme yielding unsaturated disaccharides as the end products. The facilitated diffusion effect of HCLaseM is dose-dependent in animal experiments. These properties make it a candidate for further basic research and application.

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Section: Purification and Biochemical Characterization Of Hclasemcontrasting

confidence: 98%

Cloning, Expression, and Characterization of a New Glycosaminoglycan Lyase from Microbacterium sp. H14

et al. 2019

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“…strain RM4 was small size of 25 KD. The molecular masses of several keratinases have been determined and were in the range from 18 KD for Streptomyces albidoflavus ( Bressollier et al, 1999 ) to 240 KD in Kocuria rosea ( Bernal et al, 2006 ), most keratinases have molecular weight less than 50 KD ( Suntornsuk and Suntornsuk, 2003 ; Syed et al, 2009 ; Tork et al, 2016 ). The majority of keratinases are monomeric enzymes; however, oligomeric keratinases are also reported ( Lee et al, 2012 ).…”

Section: Discussionmentioning

confidence: 99%

“…Keratinolytic microbes have become paramount important among the scientific interest owing to their capacity to produce specific keratinases and their subsequent significance in keratinic waste management ( Laba et al, 2015 ; Wang et al, 2015 ). In the present decade, keratinase research has gained momentum because of its additional industrial and biotechnological applications other than those in the conventional sectors of proteases ( Gupta and Ramnani, 2006 ; Tork et al, 2016 ). Poultry waste which constitutes feathers, nails, etc.…”

Section: Introductionmentioning

confidence: 99%

Production of Thermostable Organic Solvent Tolerant Keratinolytic Protease from Thermoactinomyces sp. RM4: IAA Production and Plant Growth Promotion

et al. 2016

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There are several reports about the optimization of protease production, but only few have optimized the production of organic solvent tolerant keratinolytic proteases that show remarkable exploitation in the development of the non-polluting processes in biotechnological industries. The present study was carried with aim to optimize the production of a thermostable organic solvent tolerant keratinolytic protease Thermoactinomyces sp. RM4 utilizing chicken feathers. Thermoactinomyces sp. RM4 isolated from the soil sample collected from a rice mill wasteyard site near Kashipur, Uttrakhand was identified on the basis of 16S rDNA analysis. The production of organic solvent tolerant keratinolytic protease enzyme by Thermoactinomyces sp. RM4 was optimized by varying physical culture conditions such as pH (10.0), temperature (60°C), inoculum percentage (2%), feather concentration (2%) and agitation rate (2 g) for feather degradation. The result showed that Thermoactinomyces sp. RM4 potentially produces extra-cellular thermostable organic solvent tolerant keratinolytic protease in the culture medium. Further, the feather hydrolysate from keratinase production media showed plant growth promoting activity by producing indole-3-acetic acid itself. The present findings suggest that keratinolytic protease from Thermoactinomyces sp. RM4 offers enormous industrial applications due to its organic solvent tolerant property in peptide synthesis, practical role in feather degradation and potential function in plant growth promoting activity, which might be a superior candidate to keep ecosystem healthy and functional.

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“…The enzymatic ability of keratin degrading microorganism to decompose keratin has long been interpreted as a key innovation [113]. Keratinase enzymes have molecular weights ranging from 18 to 240 kDa [114,115].…”

Section: Keratinmentioning

confidence: 99%

Keratin Waste: The Biodegradable Polymers

Kumawat¹,

Sharma²,

Sharma³

et al. 2018

Keratin

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Keratins are everywhere, from being the major components of household dust to common contaminants of laboratory protein analysis. Keratin is the major structural fibrous protein belonging to the large family of structural proteins to form hair, wool, feathers, nails, and horns of many kinds of animals and has a high concentration of cysteine, 7-20% of the total amino acid residues, that form inter-and intramolecular disulfide bonds. Keratin wastes are considered as the environmental pollutants and produced mostly from the poultry farms, slaughterhouses, and leather industries. Keratin wastes are dumped, buried, used for landfilling, or incinerated and all these actions increase the threats of environmental hazards, pollution, negatively influence the public health, and increase greenhouse gases concentration. Nature has provided planet Earth with a variety of beneficial organisms. Soil is considered as a well-known source for the growth of keratinophilic microflora (fungi and bacteria), which have the capability to degrade the keratin waste. The keratindegradation ability of keratinophilic microflora has been credited with the production of the microbial keratinase enzyme and biodegradation takes place (enzymatic degradation). So, the keratin wastes are the biodegradable polymers. Keratinase is the industrially significant enzyme that offers bioconversion of keratin waste, utilization as animal feed supplements, and dehairing agents in tannery industries and textile industries.

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Purification and partial characterization of serine-metallokeratinase from a newly isolated Bacillus pumilus NRC21

Cited by 30 publications

References 45 publications

Cloning, Expression, and Characterization of a New Glycosaminoglycan Lyase from Microbacterium sp. H14

Cloning, Expression, and Characterization of a New Glycosaminoglycan Lyase from Microbacterium sp. H14

Production of Thermostable Organic Solvent Tolerant Keratinolytic Protease from Thermoactinomyces sp. RM4: IAA Production and Plant Growth Promotion

Keratin Waste: The Biodegradable Polymers

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