Biochemical characterization of a detergent-stable serine alkaline protease from Caldicoprobacter guelmensis

Bouacem, Khelifa; Bouanane‐Darenfed, Amel; Laribi-Habchi, Hassiba; Elhoul, Mouna Ben; Hmida-Sayari, Aïda; Hacène, Hocine; Ollivier, Bernard; Fardeau, Marie-Laure; Jaouadi, Bassem; Béjar, Samír

doi:10.1016/j.ijbiomac.2015.08.011

Cited by 80 publications

(39 citation statements)

References 36 publications

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“…They could also help in the removal of proteinaceous stains that are often encountered in the laundry. Several works have reported the usefulness of alkaline proteases in the facilitation of blood stains removal from cotton cloth [59,60]. The common detergents contain hazardous chemicals for effectual washing performance which can be substituted by the enzymes in modern detergent formulations attributed to efficient washing along with being eco-friendly and fabric friendly.…”

Section: Removal Of Blood Stains From Cotton Fabricsmentioning

confidence: 99%

A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101

Benmrad

Moujehed

Elhoul

et al. 2016

International Journal of Biological Macromolecules

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Section: Removal Of Blood Stains From Cotton Fabricsmentioning

confidence: 99%

A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101

Benmrad

Moujehed

Elhoul

et al. 2016

International Journal of Biological Macromolecules

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“…strain AB1, B. circulans MTCC 7942, S. koyangensis TN650, C. guelmensis, Bacillus sp. EMB9, and B. licheniformis 3C5, displaying perceivable activity at extremists pH(s) (10-12) and temperatures (60-75°C) [16,24,[39][40][41][42]. Like other proteases reported in the literature [25,[43][44][45]49], SHG10 keratinolytic protease exhibited similar profile for pH stability under wide range of pH (6-10) for extended hours.…”

Section: Calculation Methodsmentioning

confidence: 72%

“…strain AB1, B. circulans MTCC 7942, Exiguobacterium profundum BK‐P23, S. koyangensis TN 650, Caldicoprobacter guelmensis , Bacillus sp. EMB9, and B. licheniformis 3C5) . Apparently, absence of proteolytic activity in factions eluted from the column with high ionic strength of 1 M NaCl (0–1) might confirm absence of protease isozyme of different pI(s) produced by B. licheniformis SHG10 DSM 28096 under the stated conditions.…”

Section: Discussionmentioning

confidence: 88%

“…Additionally, single bind appearance of the purified enzyme in the flow through fractions conferred two conclusions. The first one states that SHG10 keratinolytic alkaline protease has one protein subunit as the majority of other proteases of microbial origins reported in the literature till now [8,9,16,24,25,[39][40][41][42]. The last conclusion underlines the absence of protease isozymes of different molecular masses.…”

Section: Calculation Methodsmentioning

confidence: 93%

“…Enzyme assays were carried out at different temperatures degrees: 37, 50, 60, 70, 80, and 90°C. Moreover, thermostability of the enzyme at four time intervals along 1 h was tested at different temperatures (40,45,50,55, 60, and 65°C). Residual activity was determined after incubation of the enzyme at different temperatures from 40 to 65°C at time intervals along 1 h. Enzyme assays were carried out in triplicates.…”

Section: Characterization Of the Purified Enzymementioning

confidence: 99%

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SHG10 keratinolytic alkaline protease from Bacillus licheniformis SHG10 DSM 28096: Robust stability and unusual non‐cumbersome purification

Embaby

Saeed

Hussein

2016

J. Basic Microbiol.

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Present study underlines an unusual non-cumbersome-powerful strategy for purification of SHG10 keratinolytic alkaline protease from Bacillus licheniformis SHG10 DSM 28096 with robust stability properties. The enzyme was impressively purified to homogeneity with specific activity, purification fold, and yield of 613.82 U mg , 58.91 and 99%, respectively, via a sequential two-step purification strategy: precipitation with 65% (NH ) SO and flow through fractions of DEAE-cellulose DE 53 column. SDS-PAGE conferred a monomeric enzyme with a molecular mass of 30.4 kDa. The enzyme demonstrated optimal activity at pH (10.0-11.0) and at 65 °C. It exhibited full stability at pH (6.0-11.0) over 38 h at 4 °C and at 65 °C for 15 min. Remarkable enhanced enzyme activity (130.15 and 126.37%) was retained in presence of commercial laundry detergents Oxi and Ariel after 1 h, respectively. Organic solvent stability of the enzyme was verified in butanol, ether, acetonitrile, isopropanol, and chloroform. Imposingly, full storage stability (100%) of the enzyme along 1 year in -20 °C was confirmed. K -V was 0.00174 mM-534.2 mM Sub · min · mg protein and 1.266 mg-28.89 mg Sub · h · mg protein on N-Suc-Ala-Ala-Pro-Phe-pNA and keratin azure, respectively. Robust stability properties of SHG10 keratinolytic alkaline protease along with rapid-efficient purification underpin its potential commercialization for industrial exploitation.

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Evaluation of a novel purified and characterized alkaline protease from the extremophile Exiguobacterium alkaliphilum VLP1 as a detergent additive

Hemsinli,

Gurkok

2023

Biotechnology Journal

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This study focused on the isolation and identification of a novel alkaline protease‐producing strain from Lake Van, the largest soda lake on Earth. The objective was to purify, characterize, and investigate the potential application of protease in the detergent industry. Through a combination of classical and molecular methods, the most potent protease producer was identified as Exiguobacterium alkaliphilum VLP1. The purification process, involving ammonium sulfate precipitation, ultrafiltration, and anion exchange chromatography, resulted in a 45‐fold purification with a yield of 6.4% and specific activity of 1169 U mg−1 protein. The enzyme exhibited a molecular weight of 69 kDa, a Km value of 0.4 mm, and a maximal velocity (Vmax) value of 2000 U mg−1. The optimum activity was observed at 40°C and potential of hydrogen (pH) 9, while the enzyme also exhibited remarkable stability in the ranges of 30–60°C and pH 9–12. Notably, this study represents the first report of an alkaline protease isolated and characterized from E. alkaliphilum. This study also highlighted the potential of the enzyme as a detergent additive, as it showed compatibility with commercial detergents and effectively removed blood and chocolate stains from fabrics.

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Biochemical characterization of a detergent-stable serine alkaline protease from Caldicoprobacter guelmensis

Cited by 80 publications

References 36 publications

A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101

A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101

SHG10 keratinolytic alkaline protease from Bacillus licheniformis SHG10 DSM 28096: Robust stability and unusual non‐cumbersome purification

Evaluation of a novel purified and characterized alkaline protease from the extremophile Exiguobacterium alkaliphilum VLP1 as a detergent additive

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