Biochemical and structural characterization of a detergent-stable serine alkaline protease from seawater haloalkaliphilic bacteria

Raval, Vikram H.; Pillai, Sumitha; Rawal, C. M.; Singh, Satya P.

doi:10.1016/j.procbio.2014.03.014

Cited by 86 publications

(45 citation statements)

References 33 publications

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“…The looming climate catastrophe and global concerns for the environment have fostered the investigation of enzymes as replacements for chemical catalysts in various biochemical processes (Jain et al 2012;Raval et al 2014). Therefore, over the past decade, the application of enzymes in industrial processes has significantly increased.…”

Section: Introductionmentioning

confidence: 99%

“…Therefore, over the past decade, the application of enzymes in industrial processes has significantly increased. In 2010, the global markets for industrial enzymes were close to $3.3 billion and are expected to reach $4.4 billion by 2015 (Raval et al 2014). Within the enzyme market, proteases alone contribute to approximately 60 % of the total sales in the world, and microbial proteases constitute approximately 40 % of the total worldwide production of enzymes (George et al 2014;Ertan et al 2015).…”

Section: Introductionmentioning

confidence: 99%

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Detergent-, solvent- and salt-compatible thermoactive alkaline serine protease from halotolerant alkaliphilic Bacillus sp. NPST-AK15: purification and characterization

et al. 2015

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Alkaline protease produced by the halotolerant alkaliphilic Bacillus sp. strain NPST-AK15 was purified to homogeneity by the combination of ammonium sulfate precipitation, anion-exchange and gel permeation chromatography. The purified enzyme was a monomeric protein with an estimated molecular weight of 32 kDa. NPST-AK15 protease was highly active and stable over a wide pH range, with a maximal activity at pH 10.5. The enzyme showed optimum activity at 60 °C and was stable at 30-50 °C for at least 1 h. Thermal stability of the purified protease was substantially improved by CaCl2 (1.1- to 6.6-fold). The K m, V max and k cat values for the enzyme were 2.5 mg ml(-1), 42.5 µM min(-1) mg(-1), and 392.46 × 10(3) min(-1), respectively. NPST-AK15 protease activity was strongly inhibited by PMSF, suggesting that the enzyme is a serine protease. The enzyme was highly stable in NaCl up to 20 % (w/v). Moreover, the purified enzyme was stable in several organic solvents such as diethyl ether, benzene, toluene, and chloroform. In addition, it showed high stability and compatibility with a wide range of surfactants and commercial detergents and was slightly activated by hydrogen peroxide. These features of NPST-AK15 protease make this enzyme a promising candidate for application in the laundry and pharmaceutical industries.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Detergent-, solvent- and salt-compatible thermoactive alkaline serine protease from halotolerant alkaliphilic Bacillus sp. NPST-AK15: purification and characterization

et al. 2015

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“…Amylases with pH optimum of 9-12 have been identified in several alkaliphilic Bacillus spp. (Wang et al, 2006;Fujinami et al, 2010;Raval et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

Physiology and Molecular Phylogeny of Bacteria Isolated from Alkaline Distillery Lime

Kalwasińska¹,

Felföldi²,

Walczak³

et al. 2015

Pol J Microbiol

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A b s t r a c tThis paper presents the results of the research on the number, taxonomic composition, and biochemical properties of bacterial strains isolated from the alkaline Solvay distillery lime, deposited at the repository in Janikowo (central Poland). Fifteen strains out of 17 were facultative alkaliphiles and moderate halophiles, and two were alkalitolerants and moderate halophiles. The number of aerobic bacteria cultured in alkaline lime was approximately 10 5 CFU ml -1 , and the total number of bacteria was 10 7 cells g -1 . According to 16S rRNA gene sequence analysis, nine strains belonged to the genus Bacillus, six to the genus Halomonas, one to the genus Planococcus, and one to the genus Microcella. Strains that hydrolyse starch and protein were the most numerous. Esterase (C4) and esterase lipase (C8) were detected in the majority of bacterial strains. Twelve strains exhibited α-glucosidase activity and nine, naphtol-AS-BI-phosphohydrolase activity. The present study proves that alkaliphilic bacteria of this type may constitute a source of potentially useful extremozymes.K e y w o r d s: Bacillus sp., Halomonas sp., alkaline solvay distillery lime, alkaliphiles, halophiles

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“…Among alkaline protease-producing bacteria, there are neutralophilic, alkalotolerant, and alkaliphilic strains (Ellaiah et al 2002 ;Fujinami and Fujisawa 2010 ). Extremophilic bacteria adapted to more than one environmental stressor, such as haloalkaliphiles , which survive under saline and alkaline conditions, also produce alkaline proteases (Raval et al 2014 ). Thermophilic alkaliphiles, thermophilic haloalkaliphiles , and psychrophilic and psychrotrophic bacteria have also been reported to produce valuable alkaline proteases (Kasana 2010 ;Shrinivas and Naik 2011 ).…”

Section: Bacterial Alkaline Proteasesmentioning

confidence: 99%

Alkaline Proteases from Patagonian Bacteria

Olivera

Iglesias

Sequeiros

2016

Biology and Biotechnology of Patagonian Microorganisms

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In addition to their ecological importance in the acquisition of nitrogenrich organic compounds, extracellular proteases also have interesting biotechnological applications. Particularly, alkaline proteases represent one of the most important groups of commercial enzymes. First, we introduce the classifi cation and catalytic mechanisms of proteases. Then, this chapter reviews the advances in the bioprospection of alkaline proteases produced by bacteria adapted to selective conditions from different environments of Patagonia (Argentina). Among them, the arid soils of the Patagonian Monte are propitious for the development of alkaliphilic microorganisms. Thus, we focus on the description of the species Bacillus patagoniensis and the biochemical and catalytic properties of its alkaline protease. Then, we discuss investigations about alkaline protease-producing bacteria from the southern Patagonian coast, the prevalence of psychrophilic and psychrotolerant strains, and the response of their extracellular proteases to temperature.

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Biochemical and structural characterization of a detergent-stable serine alkaline protease from seawater haloalkaliphilic bacteria

Cited by 86 publications

References 33 publications

Detergent-, solvent- and salt-compatible thermoactive alkaline serine protease from halotolerant alkaliphilic Bacillus sp. NPST-AK15: purification and characterization

Detergent-, solvent- and salt-compatible thermoactive alkaline serine protease from halotolerant alkaliphilic Bacillus sp. NPST-AK15: purification and characterization

Physiology and Molecular Phylogeny of Bacteria Isolated from Alkaline Distillery Lime

Alkaline Proteases from Patagonian Bacteria

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