Production and Characterization of Keratinolytic Protease from New Wool-Degrading<i>Bacillus</i>Species Isolated from Egyptian Ecosystem

Hassan, Mohamed A.; Haroun, Bakry M.; Amara, Amro Abd Al Fattah; Serour, Ehab A.

doi:10.1155/2013/175012

Cited by 52 publications

(32 citation statements)

References 43 publications

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“…Similar reports were made in case of B. amyloliquefaciens MA20 and for B. cereus [22,23]. The Bacillus subtilis VCDA isolated from C. diffusa showed an optimum 48 U/ml activity at temperature 40°C Anand et al, isolated Halobacterium sp.…”

Section: Discussionsupporting

confidence: 65%

Production of Protease Showing Antibacterial Activity by Bacillus subtilis VCDA Associated with Tropical Marine Sponge Callyspongia diffusa

Rs¹,

Ap²,

Thankamani³

et al. 2017

J Microb Biochem Technol

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Section: Discussionsupporting

confidence: 65%

Production of Protease Showing Antibacterial Activity by Bacillus subtilis VCDA Associated with Tropical Marine Sponge Callyspongia diffusa

Rs¹,

Ap²,

Thankamani³

et al. 2017

J Microb Biochem Technol

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“…Keratinases are usually active in alkaline conditions and reported pH optima ranges from pH 8.0 to 10.0 [36,74,95,132] with exception of acidic pH optima which is usually found in case of keratinases from fungal sources and extremely basic pH optima also exists. [52,133] Nam et al, [48] reported that keratinase from Fervidobacterium islandicum AW-1 with a temperature optima of 100 C, is one of the most thermostable keratinases reported to date. Temperature optima of keratinases range from 40 to 80 C, as reported by various workers.…”

Section: Keratinases: Biochemical Propertiesmentioning

confidence: 99%

Microbial keratinases: industrial enzymes with waste management potential

Verma¹,

Singh

Anwar

et al. 2016

Critical Reviews in Biotechnology

127

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Proteases are ubiquitous enzymes that occur in various biological systems ranging from microorganisms to higher organisms. Microbial proteases are largely utilized in various established industrial processes. Despite their numerous industrial applications, they are not efficient in hydrolysis of recalcitrant, protein-rich keratinous wastes which result in environmental pollution and health hazards. This paved the way for the search of keratinolytic microorganisms having the ability to hydrolyze "hard to degrade" keratinous wastes. This new class of proteases is known as "keratinases". Due to their specificity, keratinases have an advantage over normal proteases and have replaced them in many industrial applications, such as nematicidal agents, nitrogenous fertilizer production from keratinous waste, animal feed and biofuel production. Keratinases have also replaced the normal proteases in the leather industry and detergent additive application due to their better performance. They have also been proved efficient in prion protein degradation. Above all, one of the major hurdles of enzyme industrial applications (cost effective production) can be achieved by using keratinous waste biomass, such as chicken feathers and hairs as fermentation substrate. Use of these low cost waste materials serves dual purposes: to reduce the fermentation cost for enzyme production as well as reducing the environmental waste load. The advent of keratinases has given new direction for waste management with industrial applications giving rise to green technology for sustainable development.

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“…Thereafter, it decreased slowly to the minimum at 9.0. Another study reported similar optimum pH for protease production (36). Furthermore, there were also reports that the best pH for protease production was 8.0(37), 9.0 (38), 10.0 (39), and 11.0 (38,40).…”

Section: Optimization Of Culture Conditions For Proteasementioning

confidence: 71%

Simultaneous Production of Β-glucanase and Protease From Bacillus Velezensis Strain Identified in the Manure of Piglets.

Khalid¹,

Miao²,

Wei³

et al. 2020

Preprint

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Background: β-glucanase and protease, are the representative of most worldwide enzyme market. In this study, a strain producing β-glucanase and protease, identified as one type of Bacillus velezensis and named Y1, was isolated from the manure of piglet.Results:Its optimal β-glucanase-producing conditions were as: fermentation temperature of 37 °C, fermentation time of 60 h, initial pH of 6.0, outfit fluid amount of 50 mL/250 mL and carbon to nitrogen ratio was 1:1. The properties of the β-glucanasewere that the most suitable reaction temperature was 65°C, the optimum pH was pH 6.0. The optimal protease-producing conditions were fermentation temperature of 37 °C, fermentation time of 60 h, initial pH of 7.0, outfit fluid amount of 75/250 mL and carbon to nitrogen ratio of 2:3.The properties of the protease showed that the most suitable reaction temperature was 50°C, the optimum pH was 6.0. And the enzyme had the best stability at 45°Cand pH 7.0. The effects of each factor on producing β-glucanase and protease by B. velezensis Y1 were as follows: temperature > time > pH > loaded liquid volume. The amplified PCR fragments of β-glucanase and protease were 1434 bp containing an open reading frame of 1413 bp encoding a protein with 444 amino acids and 1752 bp containing an open reading frame of 1521 bp encoding a protein with 506 amino acids, respectively.Conclusion: This study identified the enzymes production, optimized the fermentation conditions of β-glucanase and protease by B. velezensis. As well as the enzyme properties were investigated and genes were cloned.

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Production and Characterization of Keratinolytic Protease from New Wool-DegradingBacillusSpecies Isolated from Egyptian Ecosystem

Cited by 52 publications

References 43 publications

Production of Protease Showing Antibacterial Activity by Bacillus subtilis VCDA Associated with Tropical Marine Sponge Callyspongia diffusa

Production of Protease Showing Antibacterial Activity by Bacillus subtilis VCDA Associated with Tropical Marine Sponge Callyspongia diffusa

Microbial keratinases: industrial enzymes with waste management potential

Simultaneous Production of Β-glucanase and Protease From Bacillus Velezensis Strain Identified in the Manure of Piglets.

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