Purification and characterization of an alkaline protease from Oerskovia xanthineolytica TK-1

Saeki, Kazuo; Iwata, Junko; Watanabe, Yasuo; Tamai, Youichi

doi:10.1016/0922-338x(94)90128-7

Cited by 12 publications

(9 citation statements)

References 13 publications

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“…that presents the maximum activity at pH 8.0 to 9.0 (8,11,21). Proteases from Actinomycetes Arthrobacter luteus, Arthrobacter sp and Oerskovia xanthineolytica presented high activity at pH 10.5, 11.0 and 9.5-11.0, respectively (1,6,19). …”

Section: Resultsmentioning

confidence: 99%

Production of alkaline protease from Cellulosimicrobium cellulans

Ferracini-Santos¹,

Sato²

2009

Braz. J. Microbiol.

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Cellulosimicrobium cellulans is one of the microorganisms that produces a wide variety of yeast cell wall-degrading enzymes, β-1,3-glucanase, protease and chitinase. Dried cells of Saccharomyces cerevisiae were used as carbon and nitrogen source for cell growth and protease production. The medium components KH2PO4, KOH and dried yeast cells showed a significant effect (p<0.05) on the factorial fractional design. A second design was prepared using two factors: pH and percentage of dried yeast cells. The results showed that the culture medium for the maximum production of protease was 0.2 g/l of MgSO4.7H2O, 2.0 g/l of (NH4)2SO4 and 8% of dried yeast cells in 0.15M phosphate buffer at pH 8.0. The maximum alkaline protease production was 7.0 ± 0.27 U/ml over the center point. Crude protease showed best activity at 50ºC and pH 7.0-8.0, and was stable at 50ºC.

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Section: Resultsmentioning

confidence: 99%

Production of alkaline protease from Cellulosimicrobium cellulans

Ferracini-Santos¹,

Sato²

2009

Braz. J. Microbiol.

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Section: Discussionmentioning

confidence: 98%

“…Unlike some alkaline proteases previously reported in the literature that being moderately SDS inhibited (BM15 protease retained 70 and 56% of its activity in presence of 0.05 and 0.4% SDS, respectively) [45] or completely SDS inhibited (proteases from Oerskovia xanthineolytica TK-1 and Streptomyces sp. YSA-130 in presence of 0.1% SDS) [47,48], SHG10 keratinolytic alkaline protease was superior as it could retain 97% AE 0.99 and 89.5% AE 2.4 of its activity at 0.5 and 1% SDS, respectively. Impressively, SHG10 keratinolytic alkaline protease was not only fully stable (100%) with all tested commercial laundry detergents but also was significantly activated in presence two commercial laundry detergents (Oxi and Ariel) by 130.15 AE 1.1 and 126.47 AE 1.2%, respectively.…”

Section: Calculation Methodsmentioning

confidence: 97%

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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“…sulfurea [42] Microbacterium sp. [43] Nocardiopsisdassonvillei [44,45] Oerskoviaxanthineolytica TK-1 [46] Pimelobacter sp. 2483 [47] Pseudomonas aeruginosa [48] Pseudomonas maltophilia [49] Pseudomonas sp.…”

Section: Organism Referencesmentioning

confidence: 99%

Versatility of microbial proteases

Veloorvalappil¹,

Robinson²,

Pradeep³

et al. 2013

AER

115

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Proteases or peptidases constitute the largest group of enzymes in bio-industry with a long array of uses. They play an invincible role in industrial biotechnology, especially in detergent, food and pharmaceutical arena. This focused review encompasses an overview on alkaline proteases, mainly of microbial sources in a handy module. Following an introduction and general classification with evolutionary insight, major sources of proteases (animal, plant and microbial including fungal, bacterial), their general properties with mechanism of action and molecular masses are discussed. Proteases from Bacillus spp. have been given special attention. In addition to this, an overview on the applications of proteases in detergent, tannery, food, metal recovery and waste treatment industries is also addressed briefly.

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Purification and characterization of an alkaline protease from Oerskovia xanthineolytica TK-1

Cited by 12 publications

References 13 publications

Production of alkaline protease from Cellulosimicrobium cellulans

Production of alkaline protease from Cellulosimicrobium cellulans

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

Versatility of microbial proteases

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