The use of chemicals around the globe in different industries has increased tremendously, affecting the health of people. The modern world intends to replace these noxious chemicals with environmental friendly products for the betterment of life on the planet. Establishing enzymatic processes in spite of chemical processes has been a prime objective of scientists. Various enzymes, specifically microbial proteases, are the most essentially used in different corporate sectors, such as textile, detergent, leather, feed, waste, and others. Proteases with respect to physiological and commercial roles hold a pivotal position. As they are performing synthetic and degradative functions, proteases are found ubiquitously, such as in plants, animals, and microbes. Among different producers of proteases, Bacillus sp. are mostly commercially exploited microbes for proteases. Proteases are successfully considered as an alternative to chemicals and an eco-friendly indicator for nature or the surroundings. The evolutionary relationship among acidic, neutral, and alkaline proteases has been analyzed based on their protein sequences, but there remains a lack of information that regulates the diversity in their specificity. Researchers are looking for microbial proteases as they can tolerate harsh conditions, ways to prevent autoproteolytic activity, stability in optimum pH, and substrate specificity. The current review focuses on the comparison among different proteases and the current problems faced during production and application at the industrial level. Deciphering these issues would enable us to promote microbial proteases economically and commercially around the world.

/pdf/microbial-proteases-applications-o4nt9ikd6n.pdf

Microbial Proteases Applications.

https://www.scielo.br/pdf/bjm/v46n2/1517-8382-bjm-46-2-337.pdf

A biotechnology perspective of fungal proteases

Proteases have a broad range of applications in industrial processes and products and are representative of most worldwide enzyme sales. The genus Bacillus is probably the most important bacterial source of proteases and is capable of producing high yields of neutral and alkaline proteolytic enzymes with remarkable properties, such as high stability towards extreme temperatures, pH, organic solvents, detergents and oxidizing compounds. Therefore, several strategies have been developed for the cost-effective production of Bacillus proteases, including optimization of the fermentation parameters. Moreover, there are many studies on the use of low-cost substrates for submerged and solid state fermentation. Other alternatives include genetic tools such as protein engineering in order to obtain more active and stable proteases and strain engineering to better secrete recombinant proteases from Bacillus through homologous and heterologous protein expression. There has been extensive research on proteases because of the broad number of applications for these enzymes, such as in detergent formulations for the removal of blood stains from fabrics, production of bioactive peptides, food processing, enantioselective reactions, and dehairing of skins. Moreover, many commercial proteases have been characterized and purified from different Bacillus species. Therefore, this review highlights the production, purification, characterization, and application of proteases from a number of Bacillus species.

An overview of Bacillus proteases: from production to application.

Enzymes are widely applied in various industrial applications and processes, including the food and beverage, animal feed, textile, detergent and medical industries. Enzymes screened from natural origins are often engineered before entering the market place because their native forms do not meet the requirements for industrial application. Protein engineering is concerned with the design and construction of novel enzymes with tailored functional properties, including stability, catalytic activity, reaction product inhibition and substrate specificity. Two broad approaches have been used for enzyme engineering, namely, rational design and directed evolution. The powerful and revolutionary techniques so far developed for protein engineering provide excellent opportunities for the design of industrial enzymes with specific properties and production of high-value products at lower production costs. The present review seeks to highlight the major fields of enzyme application and to provide an updated overview on previous protein engineering studies wherein natural enzymes were modified to meet the operational conditions required for industrial application.

Biocatalysts: application and engineering for industrial purposes.

Microbial proteases: Production and application in obtaining protein hydrolysates.

Biochemical and molecular characterization of a detergent-stable serine alkaline protease from Bacillus pumilus CBS with high catalytic efficiency.

Enhancement of the thermostability and the catalytic efficiency of Bacillus pumilus CBS protease by site-directed mutagenesis

Exploring the acidotolerance of β-galactosidase from Lactobacillus delbrueckii subsp. bulgaricus: an attractive enzyme for lactose bioconversion

Enzymes have long been used as alternatives to chemicals to improve the efficiency and cost-effectiveness of a wide range of industrial systems and processes. They are currently used in basic and applied arenas of research as well as in a wide range of product design and manufacturing processes, such as those pertaining to the food, beverage, pharmaceutical, detergent, leather processing, and peptide synthesis industries (Gupta et al., 2002). Of particular interest to the aims of the present work, proteases have often been reported to constitute a resourceful class of enzymes with promising industrial applications. According to recent estimates, these enzymes account for nearly 65% of total worldwide enzyme sales (Anonyme, 2007; Rao et al., 1998). They are widely distributed in nature and play a vital role in life processes. They are particularly known for their capacity to hydrolyze peptide bonds in aqueous environments and to synthesize peptide bonds in non-aqueous biocatalysis. Proteases have been employed in a wide array of applications for many years with satisfactory results. They constitute a large family of enzymes present in a wide range of living organisms, such as plants, animals and microorganisms. In biotechnologically oriented systems and processes, however, proteases from microbial origins have often been reported to have distinct advantages when compared to plant or animal proteases, particularly because they possess almost all the characteristics desired for biotechnological applications. Among these biocatalysts, high-alkaline proteases, which alone account for about 40% of the total worldwide enzyme sales (Kirk et al., 2002), proved particularly suitable for industrial use. This is mainly due to their high stability and activity under harsh conditions.

/pdf/the-bioengineering-and-industrial-applications-of-bacterial-2f7cn2p1pl.pdf

The Bioengineering and Industrial Applications of Bacterial Alkaline Proteases: the Case of SAPB and KERAB

Characterization of an original serine alkaline proteinase from Bacillus pumilus CBS

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