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.

To produce environmental eco-friendly products and product out puts chemical process are being replaced by enzymes like proteases (Abebe et al., 2014). The production of enzymes is central to the modern biotechnology industry. The technology for producing and using commercially important enzyme products combines the discipline of microbiology, genetics, biochemistry and engineering (Rajni Hatti Kaul).Enzymes are biocatalysts produced by living cells to bring about specific biochemical reaction generally forming parts of the metabolic processes of cells (Mohammad B D et al.2013).Proteases, one among the three largest groups of industrial enzymes, account for about 60% of the worldwide sale of enzymes(Nurullal A et al 2011). Proteases which include proteinases, peptidases or proteolytic enzymes break peptide bonds between amino acids of proteins. They use a molecule of water for this and are thus classified as hydrolases.Proteases are of two ISSN: 2319-7706 Volume 4 Number 8 (2015) pp. 597-606 http://www.ijcmas.com

https://www.ijcmas.com/vol-4-8/Dalal%20Rupali,%20et%20al.pdf

Screening and Isolation of Protease Producing Bacteria from Soil Collected from Different Areas of Burhanpur Region (MP) India

Enzymes are the catalytic cornerstones of metabolic activities of living being and catalyze most of the reactions in living organisms. Microbes secrete proteases to hydrolyze the peptide bonds in proteins and therefore break the proteins down into their constituent monomers. Bacterial alkaline proteases are characterized by their high activity at alkaline pH and their broad substrate specificity. Their optimal temperature is around 60°C. These properties of bacterial alkaline proteases make them suitable for use in the detergent industry and other commercial fields. Appropriate nutritional environments must be created and maintained to ensure optimized yields and product quality. Culture media optimization is a critical step in fermentation process development and often continues throughout the production life of the fermentation product. In this study International Journal of Current Microbiology and Applied Sciences ISSN: 2319-7706 Volume 5 Number 5 (2016) pp. 767-787 Journal homepage: http://www.ijcmas.com

Screening and Characterization of Alkaline Protease Producing Bacillus Strain B-4 Bacillus flexus and Study of its Potential for Alkaline Protease Production

Production, purification and characterization of lichenin from Bacillus licheniformis.

Scenarios focus on the practical behavior of anaerobic decomposition systems to enhance biogas production, in addition to assure economic progression and ecological sustainability. The present study has framed to identify the potential hydrolytic bacteria from five different sources since principally the efficacy of hydrolytic bacteria determines the rate of hydrolysis of anaerobic decomposition and thereby biogas production. Among the 40 dominant bacteria isolated from diverse bases, 10 isolates were selected as efficient through preliminary screening.  Consequently, the premier enzyme activity obtained from the isolate G5 obtained from goat rumen fluid for cellulase (44.16±1.00 U/ml), protease (260.63±1.35 U/ml) and lipase (33.20 ± 0.81 U/ml). Morphological, biochemical and molecular characterization revealed that G5 is Bacillus sp. DDG5 (KM093856.1). A range of pH (7.0-7.5) and temperature (40oC) was sufficient for the highest activity of hydrolytic enzymes experienced. Biogas production using cow dung showed an improved efficiency of 9.54 % in Bacillus sp. DDG5 treated tank (70.16 ± 1.54 %) in contrast to control (58.13 ± 1.02%) at 30th day. However, this study established that Bacillus sp. DDG5 obtained from goat rumen fluid is the promising hydrolytic bacteria, since it can be applied for proficient hydrolysis of various organic materials to enhance methane production in outlook.
Int. J. Appl. Sci. Biotechnol. Vol 6(4): 386-396

/pdf/enhancement-of-substrate-decomposition-through-potential-59esqguu3l.pdf

Enhancement of Substrate Decomposition through Potential Hydrolytic Bacteria for Cumulative Biogas Production

Screening was done from soil samples collected from black cotton soil, groundnut field, milk processing unit, Kotappakonda hill area in Guntur Dist,and Tirumala in Chittur District, A.P. Indian soils are best for alkaline protease producing bacteria that resulted in isolation of 21 alkaline protease producing alkaliphilic bacterial strains. MS6 showed the highest production (110U/ml) after 48h. This isolate was identified as Bacillus licheniformis by Microbial Type Culture Collection center (MTCC) and gene bank, Institute of Microbial Technology (IMTECH), Chandigarh, India. This strain was used to examine the changes in alkaline protease production following UV irradiation. Induction of mutation in Bacillus licheniformis strain was carried out by 0, 3, 6, 9, 12, 15, 18 and 20 min with 30-W germicidal lamp that has radiation at 2540 - 2550A 0 at a distance of 15cm in dark and irradiated. A total of 17 mutants were selected. They were designated as Bl1 to Bl9 and Bl10 to Bl17. Among these only three strains viz., Bl2, Bl11, and Bl16 did exhibit high efficiency in production on the basis of relative growth production (C/G). Of the seventeen mutants of Bacillus licheniformis, ten were chosen to assay their productivity. Mutants no Bl8, Bl3, Bl16 were the most effective in enzyme production under submerged conditions being 180, 140,128U/ml respectively. Results revealed that alkaline protease activity assay under submerged culture conditions was more accurate than the relative growth production (C/G) method because there is no correlation between zone diameter and the ability to produce the enzyme in submerged cultures. High level of productivity increased with Bl8 mutant of B.licheniformis, indicating that the enzyme is to be thermo-alkaliphilic protease.

http://www.iosrphr.org/papers/v1i1/A011001014.pdf

Isolation and screening of alkaline protease producing bacteria and induction of overproducing Bacillus licheniformis mutants through UV irradiation

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Isolation and screening of alkaline protease producing bacteria and induction of overproducing Bacillus licheniformis mutants through UV irradiation