Alkaline serine protease from halotolerantBacillus licheniformis BA17

Öztürk, Selçuk; Özeren-Morgan, Müserref; Dilgimen, Aydan Salman; Denizci, Aziz Akın; Arikan, Burhan; Kazan, Dilek

doi:10.1007/bf03175603

Cited by 14 publications

(9 citation statements)

References 25 publications

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“…The activity of control was determined after dialysis against 10 mM EDTA. These results are similar to those reported for B. licheniformis MP1 and BA17 for each metal ion at 5.0 mM ( 32 , 38 ). In addition, the enzymatic activity of B. licheniformis RP1 and P003 and halophilic proteases from Bacillus spp.…”

Section: Resultssupporting

confidence: 90%

“…This result confirms that KB-SP is active and stable in the mesophilic temperature range. The optimum temperature and thermal stability of KB-SP were found to be similar to those of the halotolerant B. licheniformis BA17 with a half-life of 90 and 12 min at 50 and 60 °C, respectively (32).…”

Section: Stabilitymentioning

confidence: 79%

“…The enzymatic activity in each step was determined using 2 mM Suc-AAPF- p NA at 30 °C in 50 mM Tris-HCl (pH=7). Suc-AAPF- p NA as a synthetic peptide peptidyl- p NA was used to determine the enzymatic activity because the extracellular serine protease and alkaline protease showed the highest specificity towards Suc-AAPF- p NA ( 31 , 32 ). KB-SP was purified 8.6-fold with a (20.1±0.2) % yield and a specific activity of (15.0±0.2) U/mg in the final purification step ( Table 1 ).…”

Section: Resultsmentioning

confidence: 99%

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Purification and Characterization of a Novel Extracellular Haloprotease Vpr from Bacillus licheniformis Strain KB111

Foophow

Sittipol

Rukying

et al. 2022

Food Technol. Biotechnol. (Online)

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Research background. Halo-alkaline proteases are one of the most interesting types of commercial enzymes in various industries due to their high specific activity and stability under extreme conditions. Biochemical characterization of enzymes is an important requirement for determining their potential for application in industrial fields. Most of microbial proteases have been isolated from Bacillus spp. In this study, the purification and characterization of an extracellular haloprotease produced from Bacillus sp. KB111 strain, which was previously isolated from mangrove forest sediments are investigated for industrial applications. Experimental approach. The whole-genome of KB111 strain was identified by DNA sequencing. Its produced protease was purified by salting out and anion-exchange chromatography, characterized based on protease activity and stability using a peptide substrate, and identified by LC-MS/MS. Results and conclusions. The strain KB111 was identified as Bacillus licheniformis. The molecular mass of its extracellular protease, termed KB-SP, was estimated to be 70 kDa. The optimal pH and temperature for the activity of this protease was 7 and 50 °C, respectively while the enzyme exhibited maximal activity in the broad salinity range of 2–4 M NaCl. It was fully stable at an alkaline pH range of 7–11 at 50 °C with a half-life of 90 min. Metal ions such as K+, Ca2+ and Mg2+ could enhance the enzyme activity. Therefore, this protease indicates a high potential for the applications in the food and feed industry, as well as the waste management since it can hydrolyse protein at high alkaline pH and salt concentrations. The amino acids profiles of the purified KB-SP determined by LC-MS/MS analysis showed high score matching with the peptidase S8 of B. licheniformis LMG 17339, corresponding to the mature domain of a minor extracellular protease (Vpr). Amino acid sequence alignment and 3D structure modelling of KB-SP showed a conserved catalytic domain, a protease-associated (PA) domain, and a C-terminal domain. Novelty and scientific contribution. A novel extracellular haloprotease from B. licheniformis was purified, characterized, and identified. The purified protease was identified as being a minor extracellular protease (Vpr) and this is the first report on the halotolerance of Vpr. This protease has the ability to work in harsh conditions, with a broad alkaline pH and salinity range. Therefore, it can be useful in various applications in industrial fields.

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Section: Resultssupporting

confidence: 90%

Section: Stabilitymentioning

confidence: 79%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Purification and Characterization of a Novel Extracellular Haloprotease Vpr from Bacillus licheniformis Strain KB111

Foophow

Sittipol

Rukying

et al. 2022

Food Technol. Biotechnol. (Online)

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show abstract

“…Alkaline proteases contribute greatly in the global market of industrial enzymes (Banerjee et al, 1999). In general, microbial proteases are extracellular and would simplify the downstream processing of the enzyme as compared to proteases obtained from plant and animal sources (ÖZTÜRK et al, 2009). Despite the long list of protease producing microorganisms, only a few are considered as appropriate producers for commercial exploitation, being 'generally regarded as safe' (GRAS), non-toxic and non-pathogenic.…”

Section: Introductionmentioning

confidence: 99%

Effect of physical parameters, carbon and nitrogen sources on the production of alkaline protease from a newly isolatedBacillus pseudofirmus SVB1

2009

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-The effect of process physical parameters (initial pH of the medium, temperature and rpm of the shaking incubator) on the production of alkaline protease from a newly isolated Bacillus pseudofirmus SVB1 was studied using central composite design technique. The individual optimum levels of initial pH of the medium, temperature and rpm of the shaking incubator were found to be 9.2, 27.3 °C and 195, respectively for the production of alkaline protease (specific activity, U/mg of protein) and 11, 28.9 °C and 210, respectively for cell growth. By applying multiresponse analysis method of generalized distance approach for production and growth, the optimal levels were found to be 9.9, 28.1 °C and 202, for initial pH of the medium, temperature and rpm of the shaking incubator, respectively. After optimization, the production of alkaline protease and cell growth were enhanced by 36.23 and 44.29%, respectively. Also, the various nutritional parameters, which have significant effect on the production of alkaline protease, are delineated in the present study. Alkaline protease production was found to be influenced by media components, viz., types of C/N source and presence of metal ions. Finally an overall 6.2 fold increase in the production was achieved using casein as both carbon and nitrogen source.

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“…Öztürk et al. [40] reported complete loss of activity when their alkaline protease from Bacillus sp. strain BA17 was exposed to 1–5 mM of PMSF as observed in this study.…”

Section: Resultsmentioning

confidence: 99%

Overproduction of a thermo-stable halo-alkaline protease on agro-waste-based optimized medium through alternate combinatorial random mutagenesis of Stenotrophomonas acidaminiphila

Asitok

Ekpenyong

Takon

et al. 2022

Biotechnology Reports

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Alkaline serine protease from halotolerantBacillus licheniformis BA17

Cited by 14 publications

References 25 publications

Purification and Characterization of a Novel Extracellular Haloprotease Vpr from Bacillus licheniformis Strain KB111

Purification and Characterization of a Novel Extracellular Haloprotease Vpr from Bacillus licheniformis Strain KB111

Effect of physical parameters, carbon and nitrogen sources on the production of alkaline protease from a newly isolatedBacillus pseudofirmus SVB1

Overproduction of a thermo-stable halo-alkaline protease on agro-waste-based optimized medium through alternate combinatorial random mutagenesis of Stenotrophomonas acidaminiphila

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