Isolation and screening of an extracellular organic solvent-tolerant protease producer

Geok, Lee Poh; Razak, Che Nyonya Abdul; Rahman, Raja Noor Zaliha Abd.; Basri, Mahiran; Salleh, Abu Bakar

doi:10.1016/s1369-703x(02)00137-7

Cited by 75 publications

(53 citation statements)

References 11 publications

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“…Previous studies have reported organic solvent-tolerant strains from the genus Pseudomonas and Bacillus producing solvent stable enzymes (Fig. 12) [32,33].…”

Section: Effect Of Organic Solventsmentioning

confidence: 99%

Isolation, Purification, and Optimization of Thermophilic and Alkaliphilc Protease Originating From Hot Water Spring Bacteria

Puntambekar

Dake

2017

Asian J Pharm Clin Res

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Objective: The main objective of this study is to investigate the industrial applications of a thermophillic alkaline protease from a hot water spring bacterial isolate "A" and to study its production, optimization, and purification. Methods:The alkaline protease was produced using shake flask studies maintaining a pH of 9.0 and a temperature of 50°C. Optimization studies of the enzyme were carried out using variable pH, temperature, organic carbon, and nitrogen sources followed by purification of the enzyme using DEAE-cellulose ion exchange chromatography technique. Stability of the enzyme was analyzed in the presence of organic solvents and surfactants. The efficiency of the enzyme in the removal of proteinaceous stains in the presence of strong detergents under extreme conditions was assessed. The fibrinolytic activity of the enzyme in dissolving the blood clot was confirmed. Results:The isolated alkaline protease was purified to homogeneity with a 16-fold increase. Media optimization studies revealed that 1% glucose and 1 % casein-induced the production of alkaline protease. The purified enzyme retained stability in the presence of ethanol, methanol, and acetone and surfactants such as 0.5% (w/v) sodium dodecyl sulfate (SDS) and 0.5% (v/v) Triton-X-100. The isolated alkaline protease successfully removed the proteinaceous stains and showed significant results in the dissolution of blood clot. Conclusion:The above experimental results confirm that the isolated enzyme has both thermophilic and alkaliphilic protease properties. Thereby the enzyme finds promising industrial applications even in extreme conditions.

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“…Previous studies have reported organic solvent-tolerant strains from the genus Pseudomonas and Bacillus producing solvent stable enzymes (Fig. 12) [32,33].…”

Section: Effect Of Organic Solventsmentioning

confidence: 99%

Isolation, Purification, and Optimization of Thermophilic and Alkaliphilc Protease Originating From Hot Water Spring Bacteria

Puntambekar

Dake

2017

Asian J Pharm Clin Res

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“…Studies on enzymes from solvent tolerant microbes appear promising in this regard [209]. Some of these microbes are reported to be rich sources of industrially important proteases [95,221]. These enzymes are logically attuned to work under solvent rich environment, hence generally stable in organic solvents [209].…”

Section: Alkaline Proteases From Organic Solvent Tolerant Microbesmentioning

confidence: 99%

“…Ogino et al [95] reported, for the first time, an organic solvent-tolerant bacterium P. aeruginosa PST-01, which grew well in the presence of organic solvents such as hexane, toluene, benzene, and secreted a protease stable to various organic solvents [95,137]. Geok and co-workers [221] isolated an organic solvent-tolerant protease producer P. aeruginosa strain K out of 11 isolates of benzene-toluene-xylene-ethyl benzene tolerant bacteria. This bacterium was a polycyclic aromatic hydrocarbon degrader.…”

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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“…Xylene (85%) and benzene (67%) slightly inhibited enzyme activity at 0.5% concentration (Table 6). However, only a few studies have been made on organic solvent stable proteases, such as those from Pseudomonas aeruginosa (Ogino et al 1999;Geok et al 2003), which was stable in the presence of organic and water immiscible solvents. Metalloprotease with molecular mass of 38 kDa produced by a marine Vibrio sp.…”

Section: +mentioning

confidence: 99%

Thermostable alkaline protease from newly isolated Vibrio sp.: extraction, purification and characterisation

et al. 2012

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AbstractAn extracellular alkaline protease-producing Vibrio sp. was isolated from mangrove sediments of Vellar estuary. A 9.36-fold purification was achieved by a three-step purification procedure and the molecular weight of the enzyme was determined as 33 kDa by SDS-PAGE. The enzyme was active in a broad range of pH (6.0–11.0) and temperature (30–70°C), the optimum being at pH 9.0 and temperature 55°C. The enzyme was stable at alkaline pH range of 9–11 and up to a temperature of 60°C, after incubation for 1 h. Metals like Co2+, Hg2+, Ni2+ and Cu2+ inhibited the enzyme activity, whereas Fe2+, Ca2+ and Mn2+ were found to enhance the activity. The protease was found to be highly stable in the presence of oxidizing agents like H2O2, detergents such as SDS and Triton-X-100 and also some of the commonly used commercial detergents. The organic solvents like xylene, isopropanol, hexane and benzene were found to enhance as well as stabilize the enzyme activity. The extracellular production of the enzyme, the pH and thermal stability, and the stability in presence of oxidants, surfactants, commercial detergents and organic solvents, altogether suggest that it can be used as a laundry additive.

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Isolation and screening of an extracellular organic solvent-tolerant protease producer

Cited by 75 publications

References 11 publications

Isolation, Purification, and Optimization of Thermophilic and Alkaliphilc Protease Originating From Hot Water Spring Bacteria

Isolation, Purification, and Optimization of Thermophilic and Alkaliphilc Protease Originating From Hot Water Spring Bacteria

Extreme Environments: Goldmine of Industrially Valuable Alkali-stable Proteases

Thermostable alkaline protease from newly isolated Vibrio sp.: extraction, purification and characterisation

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