Homology modeling and heterologous expression of highly alkaline subtilisin-like serine protease from Bacillus halodurans C-125

Tekin, Aşkın; Uzuner, Uğur; Sezen, Kazım

doi:10.1007/s10529-020-03025-6

Cited by 16 publications

(9 citation statements)

References 45 publications

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“…The acquired data for the reference proteases are congruent to the data found in literature [36,57]. The pH optimum of SPAO at pH 9.0 and its working range until pH 12.0 draw attention to its great potential toward various industrial applications, similar to other alkaline proteases reported before [51,52,58]. Thus, SPAO and Savinase are not only highly alkaline subtilisins based on their amino acid sequence, but also differ clearly from BPN' and subtilisin Carlsberg with increased activity at pH 12.0.…”

Section: Effects Of Temperature and Ph On Enzyme Activity And Stabilitysupporting

confidence: 85%

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Biochemical characterization of a novel oxidatively stable, halotolerant, and high‐alkaline subtilisin from Alkalihalobacillus okhensisKh10‐101^T

et al. 2022

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Halophilic and halotolerant microorganisms represent a promising source of salt‐tolerant enzymes suitable for various biotechnological applications where high salt concentrations would otherwise limit enzymatic activity. Considering the current growing enzyme market and the need for more efficient and new biocatalysts, the present study aimed at the characterization of a high‐alkaline subtilisin from Alkalihalobacillus okhensis Kh10‐101 T . The protease gene was cloned and expressed in Bacillus subtilis DB104. The recombinant protease SPAO with 269 amino acids belongs to the subfamily of high‐alkaline subtilisins. The biochemical characteristics of purified SPAO were analyzed in comparison with subtilisin Carlsberg, Savinase, and BPN'. SPAO, a monomer with a molecular mass of 27.1 kDa, was active over a wide range of pH 6.0–12.0 and temperature 20–80 °C, optimally at pH 9.0–9.5 and 55 °C. The protease is highly oxidatively stable to hydrogen peroxide and retained 58% of residual activity when incubated at 10 °C with 5% (v/v) H 2 O 2 for 1 h while stimulated at 1% (v/v) H 2 O 2 . Furthermore, SPAO was very stable and active at NaCl concentrations up to 5.0 m . This study demonstrates the potential of SPAO for biotechnological applications in the future.

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Section: Effects Of Temperature and Ph On Enzyme Activity And Stabilitysupporting

confidence: 85%

“…SK37. The subtilisin from Bacillus halodurans C‐125 demonstrated high stability with 94% remaining activity after 1 h of incubation at 50 °C [ 52 ]. A comparable loss of activity for subtilisin Carlsberg was also observed by others [ 53 , 54 ].…”

Section: Resultsmentioning

confidence: 99%

Biochemical characterization of a novel oxidatively stable, halotolerant, and high‐alkaline subtilisin from Alkalihalobacillus okhensisKh10‐101^T

et al. 2022

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“…While, the optimal pH of an alkaline protease from Bacillus halodurans C-125 is 12.0 (Tekin et al, 2021). For pH stability, AprBcp exhibited high residual activity (above 80%) in the range from pH 8.0 to 11.0 after 5 h of incubating at 25°C (Figure 4B), which is similar to previous reported alkaline protease (Rajkumar et al, 2011;Jagadeesan et al, 2020;Tekin et al, 2021).…”

Section: Characterization Of Aprbcpsupporting

confidence: 87%

“…The maximum activities of alkaline proteases from B. pumilus AR57 and Bacillus megaterium RRM2 are detected at 9.0 and 10.0, respectively (Rajkumar et al, 2011;Jagadeesan et al, 2020). While, the optimal pH of an alkaline protease from Bacillus halodurans C-125 is 12.0 (Tekin et al, 2021). For pH stability, AprBcp exhibited high residual activity (above 80%) in the range from pH 8.0 to 11.0 after 5 h of incubating at 25°C (Figure 4B), which is similar to previous reported alkaline protease (Rajkumar et al, 2011;Jagadeesan et al, 2020;Tekin et al, 2021).…”

Section: Characterization Of Aprbcpmentioning

confidence: 96%

Overexpression of Bacillus circulans alkaline protease in Bacillus subtilis and its potential application for recovery of protein from soybean dregs

Chen

Huang

et al. 2022

Front. Microbiol.

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Proteases are important for decomposition of proteins to generate peptides or amino acids and have a broad range of applications in different industries. Herein, a gene encoding an alkaline protease (AprBcp) from Bacillus circulans R1 was cloned and bioinformatics analyzed. In addition, a series of strategies were applied to achieve high-level expression of AprBcp in Bacillus subtilis. The maximum activity of AprBcp reached 165,870 U/ml after 60 h fed-batch cultivation in 50 l bioreactor. The purified recombinant AprBcp exhibited maximum activity at 60°C and pH 10.0, and remained stable in the range from pH 8.0 to 11.0 and 30 to 45°C. Metal ions Ca2+, Mn2+, and Mg2+ could improve the stability of AprBcp. Furthermore, the recombinant AprBcp displayed great potential application on the recovery of protein from soybean dregs. The results of this study will provide an effective method to prepare AprBcp in B. subtilis and its potential application on utilization of soybean dregs.

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“…Serene proteases produced by Bacillus sp. and alkaline proteases by some fungal strains widely used in detergent formulations due to their ease of manufacturing, down streaming are gaining prominence in detergent industry (Tekin et al 2020 ). Protease produced by Bacillus licheniformis RP1 has been identified as a strong detergent ingredient with stable action in a solution of 10% (w/v) commercial detergent (Fabs Perfect), implying its commercial use.…”

Section: Microbial Proteases and Its Industrial Applicationsmentioning

confidence: 99%

Microbial proteases: ubiquitous enzymes with innumerable uses

Solanki

Putatunda²,

Bhatia

et al. 2021

3 Biotech

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Proteases are ubiquitous enzymes, having significant physiological roles in both synthesis and degradation. The use of microbial proteases in food fermentation is an age-old process, which is today being successfully employed in other industries with the advent of ‘omics’ era and innovations in genetic and protein engineering approaches. Proteases have found application in industries besides food, like leather, textiles, detergent, waste management, agriculture, animal husbandry, cosmetics, and pharmaceutics. With the rising demands and applications, researchers are exploring various approaches to discover, redesign, or artificially synthesize enzymes with better applicability in the industrial processes. These enzymes offer a sustainable and environmentally safer option, besides possessing economic and commercial value. Various bacterial and fungal proteases are already holding a commercially pivotal role in the industry. The current review summarizes the characteristics and types of proteases, microbial source, their current and prospective applications in various industries, and future challenges. Promoting these biocatalysts will prove significant in betterment of the modern world.

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Homology modeling and heterologous expression of highly alkaline subtilisin-like serine protease from Bacillus halodurans C-125

Cited by 16 publications

References 45 publications

Biochemical characterization of a novel oxidatively stable, halotolerant, and high‐alkaline subtilisin from Alkalihalobacillus okhensisKh10‐101^T

Biochemical characterization of a novel oxidatively stable, halotolerant, and high‐alkaline subtilisin from Alkalihalobacillus okhensisKh10‐101^T

Overexpression of Bacillus circulans alkaline protease in Bacillus subtilis and its potential application for recovery of protein from soybean dregs

Microbial proteases: ubiquitous enzymes with innumerable uses

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Homology modeling and heterologous expression of highly alkaline subtilisin-like serine protease from Bacillus halodurans C-125

Cited by 16 publications

References 45 publications

Biochemical characterization of a novel oxidatively stable, halotolerant, and high‐alkaline subtilisin from Alkalihalobacillus okhensisKh10‐101T

Biochemical characterization of a novel oxidatively stable, halotolerant, and high‐alkaline subtilisin from Alkalihalobacillus okhensisKh10‐101T

Overexpression of Bacillus circulans alkaline protease in Bacillus subtilis and its potential application for recovery of protein from soybean dregs

Microbial proteases: ubiquitous enzymes with innumerable uses

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Biochemical characterization of a novel oxidatively stable, halotolerant, and high‐alkaline subtilisin from Alkalihalobacillus okhensisKh10‐101^T

Biochemical characterization of a novel oxidatively stable, halotolerant, and high‐alkaline subtilisin from Alkalihalobacillus okhensisKh10‐101^T