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Psychrophilic Enzymes Adaptations and Industrial Relevance
Published in Pratibha Dheeran, Sachin Kumar, Extremophiles, 2022
Shivika Sharma, Vikas Sharma, Subhankar Chatterjee, Sachin Kumar
Enzymes have a major dominance in the market of detergent formulation and are very actively used in detergent industry across the globe. In the current trend, the utilization of detergents at lower temperature washing conditions is very actively employed because of decreased energy consumption, reduced cost infrastructure and for the maintenance of texture of fabrics. Among various enzymatic agents, subtilisin which is an alkaline serine protease isolated from Bacillus species mainly rules detergent industry (Feller 2012). Accordingly, psychrophilic subtilisins are being actively developed for washing at moderate temperature conditions. To achieve this goal, the first cold active subtilisin isolated from psychrophilic Bacillus species from Antarctic continent has been produced to cope up with the demand of detergent industry (Narinx et al. 1997). The cold active detergents containing engineered cold active subtilisin have various advantages such as alkaline stability and cold activity which make them ideal contender in detergent formulation.
Genetic Strategies for Strain Improvement
Published in Daphne L. Stoner, Biotechnology for the Treatment of Hazardous Waste, 2017
More successful in some instances has been the rational redesign of enzymes or enzyme systems based on information regarding the amino acid sequences involved in enzyme stability. Recently, the technique of site directed mutagenesis has been used to markedly increase the stability of the commercially useful enzyme subtilisin.28,29 By changing amino acid residues subject to inactivation by temperature or proteolysis, the stability the subtilisin molecule was increased by an order of magnitude. While this particular enzyme has limited application in hazardous waste degradation, it serves as an example of what can be done using modern genetic strategies for improving the stability of enzymes that have cloned and well characterized genes.
Improving operational stability of thermostable Pythium myriotylum secretory serine protease by preparation of cross-linked enzyme aggregates (CLEAs)
Published in Preparative Biochemistry & Biotechnology, 2020
Aswati R. Nair, Geethu Chellapan
Global market for industrial enzymes was estimated at 5.6$billion in 2018 and this demand is expected to increase at 6.8% compound annual growth rate (CAGR) by 2024.[1] Approximately, 75% of the enzymes used in industries are hydrolases like proteases, cellulases, amylases, and lipases.[1] Proteases remain the dominant enzyme type among hydrolases[2,3] due to their extensive use in the detergent and dairy industries.[4] Among proteases, alkaline serine proteases (SPs) are the most important group of commercially exploited enzymes and account for approximately 35% of the total microbial enzyme sales.[5,6] Most of the commercial alkaline proteases viz. Subtilisin Carlsberg, Subtilisin BPN’, Alcalase, Esperase and Savinase sourced from Bacillus find major applications in detergent industry.[4,7] However these proteases exhibit some drawbacks that include instability in presence of surfactants and oxidizing agents commonly found in detergent formulations besides high production costs.[8]
Use of biostimulants obtained from okara in the bioremediation of soils polluted by imazamox
Published in Bioremediation Journal, 2022
Manuel Ortiz-Botella, Isidoro Gómez, Patricia Paneque, Pablo Caballero, Juan Parrado, Alfonso Vera, Felipe Bastida, Carlos García, Manuel Tejada
The hydrolysis process took place in a bioreactor according to the pH-stat methodology (Adler-Nissen 1977). The enzyme subtilisin was used to obtain the first biostimulant (OB). This enzyme is an endoprotease that breaks down proteins internally, generating peptides of different molecular size, but rarely does it generate free amino acids. Subtilisin was obtained by liquid fermentation with Bacillus licheniformis ATCC® 21415™. The hydrolysis lasted for 2 hours at a temperature of 55 °C, with 0.3% enzyme and under constant pH conditions adjusting with KOH (pH = 9).