Production optimization of an extracellular cold-active alkaline protease from Stenotrophomonas maltophilia MTCC 7528 and its application in detergent industry

Proteases are being an industrial candidate, which are widely used in food, bakery, and beverage and detergent industry. In leather industry, alkaline proteases are exhibiting a prominent role in unhairing and bating processes. An extensive use of filamentous fungi, especiallyAspergillus specieshas been studied elaborately. Although, the significant application of alkaline protease produced from these strains in leather industry is being limited.Aspergillus flavusandAspergillus terreusfound as the potential strains for production of tannery protease in submerged fermentation. To improve the productivity of this enzyme in liquid broth, various media ingredients have been optimized. The crude and partially purified proteases preliminarily characterized and used for unhairing processes at lab scale in tannery. The protease obtained from these strains showed the good activity in wide alkaline condition at 50 °C suggesting the possibility of using in leather and detergent industry.

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Screening, purification and characterization of a novel cold-active and organic solvent-tolerant lipase from Stenotrophomonas maltophilia CGMCC 4254

Bioresource Technology ◽

10.1016/j.biortech.2013.08.101 ◽

2013 ◽

Vol 148 ◽

pp. 114-120 ◽

Cited By ~ 46

Author(s):

Mu Li ◽

Li-Rong Yang ◽

Gang Xu ◽

Jian-Ping Wu

Keyword(s):

Organic Solvent ◽

Stenotrophomonas Maltophilia ◽

Purification And Characterization ◽

Organic Solvent Tolerant ◽

Cold Active ◽

Solvent Tolerant

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Cold-active serine alkaline protease from the psychrophilic bacterium Pseudomonas strain DY-A: enzyme purification and characterization

Extremophiles ◽

10.1007/s00792-003-0323-x ◽

2003 ◽

Vol 7 (4) ◽

pp. 335-337 ◽

Cited By ~ 48

Author(s):

Runying Zeng ◽

Rui Zhang ◽

Jing Zhao ◽

Nianwei Lin

Keyword(s):

Alkaline Protease ◽

Enzyme Purification ◽

Psychrophilic Bacterium ◽

Purification And Characterization ◽

Serine Alkaline Protease ◽

Cold Active

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ISOLATION, PURIFICATION, AND OPTIMIZATION OF THERMOPHILIC AND ALKALIPHILC PROTEASE ORIGINATING FROM HOT WATER SPRING BACTERIA

Asian Journal of Pharmaceutical and Clinical Research ◽

10.22159/ajpcr.2017.v10i9.19717 ◽

2017 ◽

Vol 10 (9) ◽

pp. 284

Author(s):

Ashwini Nilesh Puntambekar ◽

Manjusha Sudhakar Dake

Keyword(s):

Alkaline Protease ◽

Blood Clot ◽

Sodium Dodecyl ◽

Deae Cellulose ◽

Industrial Applications ◽

Exchange Chromatography ◽

Production Optimization ◽

Hot Water ◽

Extreme Conditions ◽

Water Spring

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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