Purification and characterization of a salt, solvent, detergent and bleach tolerant protease from a new gamma-Proteobacterium isolated from the marine environment of the Sundarbans

Sana, Barindra; Ghosh, Debashish; Saha, M.; Mukherjee, Joydeep

doi:10.1016/j.procbio.2005.09.010

Cited by 110 publications

(45 citation statements)

References 43 publications

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“…These results suggested that the integrity of intramolecular and/or intermolecular disulfide bonds should be involved in the proteolysis mechanism (Abidi et al 2011), and this was in accordance with the results for Ve2-20-91 protease (Raval et al 2014). On the contrary, Sana et al (2006) showed that the protease of NIOCC #20 is thiol-independent because reducing agents such as DTT and β-ME did not affect its activity considerably. Moreover, the activity of protease from Bacillus lehensis was slightly enhanced by the addition of β-ME and DTT (Joshi and Satyanarayana 2013).…”

Section: Effect Of Metal Ions and Inhibitorsmentioning

confidence: 92%

“…The activity and pH stability of NPST-AK15 protease in high alkaline conditions signify its potential applicability in the laundry industry. Generally, detergent-compatible enzymes should tolerate alkaline conditions because the pH of laundry detergents is generally in the range of 9-12, which is an important criterion for detergent-based proteases (Sana et al 2006;Jain et al 2012).…”

Section: Figmentioning

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: Effect Of Metal Ions and Inhibitorsmentioning

confidence: 92%

Section: Figmentioning

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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“…Gelatin zymography was performed in polyacrylamide slab gel containing SDS and gelatin (0.1%) as a co-polymerized substrate, as described by Sana et al (2006) but with some modifi cations. The activity band was observed as a clear colorless area depleted of gelatin in the gel against the blue background.…”

Section: Methodsmentioning

confidence: 99%

A cold-active extracellular metalloprotease from Curtobacterium luteum (MTCC 7529): Enzyme production and characterization

Kuddus

Ramteke

2008

J. Gen. Appl. Microbiol.

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A novel psychro-tolerant bacterium, Curtobacterium luteum, secreting an extracellular protease was isolated from the soil of Gangotri glacier, Western Himalaya. Maximum enzyme production was achieved when the strain was grown in a pH-neutral medium containing skim milk at 15 C over 120 h. The metal ions such as Zn 2+ and Cr 2+ enhanced enzyme production. The specifi c activity of purifi ed enzyme was 8,090 units/mg after 34.1-fold purifi cation. The 115 kDa enzyme was a metalloprotease (activity inhibited by EDTA and EGTA) and showed maximum activity at 20 C and pH 7. The enzyme was active over a broad pH range and retained 84% of its original activity between pH 6 and 8. There was no loss in enzyme activity when exposed for 3 h at 4

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“…Halophilic microorganisms generally produce salt requiring enzymes as a result of adaptation to high salt conditions. Since salt reduces water activity (a feature in common with organic solvent systems), halophilic enzymes are considered to be valuable tools as biocatalysts in aqueous-organic media [195,230,231]. A summary of organic solvent stability profile of some alkaline proteases is listed in Table 4.…”

Section: Alkaline Proteases From Organic Solvent Tolerant Microbesmentioning

confidence: 99%

Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

Garg¹,

Singh²

2015

Enz Eng

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Since the advent and release of Bio 40 (the first detergent with bacterial alkaline protease) in 1959, exploration of the microbial alkaline proteases has been exploited beyond expectations. The inventory of microbial alkaline proteases is difficult to draft as it is increasing daily. Most of these proteases are the result of studies in which one or a few isolates were targeted for an alkali-stable enzyme. Although, the worldwide research on microbial alkaline proteases has been widely performed, we still need an improved enzyme capable of catalyzing reactions under extreme conditions (also called as extremozymes), e.g., high alkalinity and salinity, anhydrous environment, cold and hot environment, etc. As the search for extremozymes is in progress, it is imperative to explore the extreme environments to get some novel microbial strains (extremophiles) for alkali-stable proteases. This review article is an effort to compile the scattered information on some extremophiles and their alkali-stable proteases, which may have better specific industrial applications. It includes: (i) various extreme environments relevant to industrial biocatalysts, (ii) strategies of extremophilic microbes and enzymes which make them able to tolerate such conditions, and (iii) an overview of some important work done so far to explore industrially relevant extremophilic enzymes from extremophiles.

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Purification and characterization of a salt, solvent, detergent and bleach tolerant protease from a new gamma-Proteobacterium isolated from the marine environment of the Sundarbans

Cited by 110 publications

References 43 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

A cold-active extracellular metalloprotease from Curtobacterium luteum (MTCC 7529): Enzyme production and characterization

Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

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