Production of an alkaline protease using <i>Bacillus pumilus</i> D3 without inactivation by SDS, its characterization and purification

Özçelik, Burçin; Aytar, Pınar; Gedikli, Serap; Yardımcı, Ezgi; Çalışkan, Figen; Çabuk, Ahmet

doi:10.3109/14756366.2013.788503

Cited by 15 publications

(12 citation statements)

References 34 publications

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“…At the optimum temperature, protease activity reached highest at 60 h of fermentation, which was identical with some other researches (33,34), and much shorter as reported by (31,32). However, the optimal fermentation time of protease for Bacillus pumilus D3 was 48 h (35). After 72 h, the enzyme activity of protease decreased gradually.…”

Section: Optimization Of Culture Conditions For Proteasesupporting

confidence: 86%

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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Section: Optimization Of Culture Conditions For Proteasesupporting

confidence: 86%

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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“…Total activity of Stenotrophomonas acidaminiphila UCCM 00065 alkaline protease was 25,950.72 U in the bioreactor study while 5,748.46 U was observed in shake flask experiments from crude total protein of 1625.29 mg and 378.65 mg respectively. Such high alkaline protease activity and total protein have earlier been reported in a few bacteria like Bacillus stereothermophilus (Karray et al 2021) and Bacillus pumilus strain MK6-5 (Ozcelik et al 2014) after employing different methods of optimization.…”

Section: Discussionsupporting

confidence: 59%

A Novel Strain of Stenotrophomonas Acidaminiphila Produces Super-active Alkaline Protease During Cassava Effluent Fermentation: Process Optimization, Kinetic Modeling and Scale-up

Asitok

Ekpenyong

Takon

et al. 2021

Preprint

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PurposeMicrobial fermentations for value-added metabolites production are exploited for efficient bioconversion of agro-industrial wastes for the dual purposes of pollution abatement and cost-effectiveness.MethodsIn the present study, the regular 2-level factorial design was employed to screen fermentation parameters that enhance production of a novel alkaline protease by a strain of Stenotrophomonas acidaminiphila using cassava processing effluent as substrate. Data from randomized experiments of central composite rotatable design for improved enzyme activity, guided by path of steepest ascent experiments, were modeled and optimized by response surface methodology (RSM). Shake flask kinetics of production under optimized conditions was modeled by logistic and modified Gompertz models and determinations of maximum specific growth rate, µmax, maximum volumetric rate of substrate consumption, rsm, maximum volumetric rate of biomass formation, rxm and specific yield of product, Yp/x were made.ResultsLogistic model poorly fitted RSM-generated product formation and substrate consumption data. However, biomass formation was accurately fitted (adjusted r2 >99%), with µmax of 0.471 h-1. The modified Gompertz model, on the contrary, more accurately fitted all three major response data with minimal mean squared error. Potential for scale-up of bioprocess evaluated in 5-L bioreactor satisfactorily revealed 8.5-fold more substrate consumption in bioreactor than in shake flask. The 86.76-fold aqueous two-phase system-purified protease had a specific activity of 1416.73 Umg-1 which improved with increasing surfactant concentration.ConclusionThese results suggest significant bioprocess potential for sustainable cassava effluent management and concomitant commercial production of alkaline protease for industrial detergent application.

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“…Protein concentrations were determined through the Bradford method (Bradford 1976). The amount of the enzyme resultant from the release of 1 mg of tyrosine each minute at 30 °C is determined as one unit of enzyme activity (Özçelik et al, 2013;Akkır et al, 2017). The strain exhibiting maximum proteolytic activity was chosen for other experiments.…”

Section: Protease Production Medium and Screening Of Proteolytic Actimentioning

confidence: 99%

HEAT AND pH STABLE PROTEASE PRODUCED BY A BACTERIUM ISOLATED FROM FIELDS WITH HIGH BORON

ŞAT¹

2021

J microb biotech food sci

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In this study, production, optimization and characterization of protease produced by a bacterium isolated from Kırka boron mine distinct were performed. The proteolytic activities of isolates were screened based on Anson method. The optimal production conditions for protease were determined by using Central Composite Design. Bacillus sp. DB14 isolate (accession number: KY110868) exhibited the highest activity in terms of protease enzyme (346.15 U/mg) among the other isolates screened. The highest result for protease activity of Bacillus sp. DB14 isolate was obtained as 481.76 U/mg according to experimental set. Optimum pH and temperature of Bacillus sp. DB14 protease were found as 10.5 and 60 °C, respectively. Interestingly, this enzyme could stand stable at the range of 20-50 °C. However, the enzyme activity started to decrease highly after 50 °C. Besides, pH stability of this enzyme was provided between pH 7 and pH 11. Inhibition of protease was observed in solution with 10 mM Ni2+, Fe3+, Hg2+, Cd2+ and B3+. Cu2+ ion was found to enhance enzyme activity. Bacillus sp. DB14 protease exhibited remarkably stability in the temperature range of 20 °C and 50 °C. Proteolytic activity values obtained at the range of pH 7-11 were stable. These results indicated that the alkaline protease from this isolate might be potential for biotechnological applications.

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Production of an alkaline protease using Bacillus pumilus D3 without inactivation by SDS, its characterization and purification

Cited by 15 publications

References 34 publications

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

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

A Novel Strain of Stenotrophomonas Acidaminiphila Produces Super-active Alkaline Protease During Cassava Effluent Fermentation: Process Optimization, Kinetic Modeling and Scale-up

HEAT AND pH STABLE PROTEASE PRODUCED BY A BACTERIUM ISOLATED FROM FIELDS WITH HIGH BORON

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