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.

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Microbial Proteases Applications.

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.

Design of novel enzyme biocatalysts for industrial bioprocess: Harnessing the power of protein engineering, high throughput screening and synthetic biology

Enzymes are the cornerstones of metabolism and constitute the fundamental basis for existence of life However, recently enzymes are being implicated in diverse industrial processes because of their specific and fast action for efficient bioconversion of substrate to product, and their capability to save raw materials, energy and chemicals for various manufacturing processes Enzymes are considered as environment-friendly (green) chemicals that may potentially help replacing completely or reducing the usage of hazardous chemicals for industrial processes, thus promising sustainable production and manufacturing Among various industrial enzymes microbial proteases dominate the world enzyme market due to their multifaceted application potential in varied bioindustries like food, pharmaceutical, textile, photographic, leather and detergent Promising applications of proteases in agricultural sector for instance may include biocontrol of pests, degumming of silk, selective delignification of hemp and wool processing However, for successful industrial applications the proteases must be robust enough to suit the process conditions which are generally hostile Proteases intended for industrial applications must have activity and stability over wide range of temperature and pH extremes for prolonged time periods and even in the presence of various potential enzyme inhibitors Of various microbial proteases those from Bacillus spp have got special significance because the latter are known for their ability to produce sturdy enzymes that might have suitability for industrial process conditions The current article presents an interpretive summary of the recent developments on application potential of proteases for various industries

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Potential application spectrum of microbial proteases for clean and green industrial production

Bacillus spp. are an affordable source of enzymes due to their wide distribution, safety in work, ease of cultivation, and susceptibility to genetic transformations. Researchers are particularly interested in proteolytic enzymes, which constitute one of the most diverse groups of microbial proteins in terms of properties. Despite the long history of their research, this group of enzymes continue to show great potential for practical application in the biomedical industry, as well as in the agricultural industry. Thus, the unique properties of bacillary proteinases, such as stability in a wide range of temperatures and pH, high specificity, biodegradability of a wide range of substrates, and the high potential of sequenced Bacillus genomes are a powerful foundation for the development of new biotechnologies. The current review aims to discuss recent studies on various enzymes in particular, proteinases produced by bacteria of the genus Bacillus, along with their prospective practical applications. This article also presents an interpretive summary of the recent developments on the usage of probiotic Bacillus strains as potential feed additives.

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The Practical Potential of Bacilli and Their Enzymes for Industrial Production

Current advances in the classification, production, properties and applications of microbial biosurfactants - A critical review.

Proteases with characteristic stabilities are considered attractive candidates for industrial catalysis. In the present study, a potent bacterial strain KT004404, an inhabitant of hydrothermal vents, was isolated and characterized for protease production. Initial screening indicated that this strain produced a hydrolytic zone of 30 mm 16S rRNA-based identification revealed that our isolate was a strain of Bacillus subtilis. Optimum reaction condition for maximum protease production was determined as 55 °C, pH 6, 1 % inoculum size and malt extract as primary growth substrate supplemented with 1 % dextrose. Yield of the enzyme was increased up to 7.53 folds with a specific activity of 55.125 U/mg after gel filtration chromatography. SDS-PAGE analysis confirmed the size of protease as 28.24 kDa. Purified enzyme retained its catalytic activity over a broad range of temperature (5 to 65 °C) and pH [5–8]. Addition of metal ions shown to have a stimulatory effect on catalytic properties while EDTA inhibited the efficiency of the enzyme confirming it as a metalloprotease. Protease exhibited excellent stability and activity in the presence of anionic surfactants, solvents, and detergents. The results of dehairing and destaining experiments suggested that the protease produced by B. subtilis KT004404 could be used in leather and textile industries with ecological benefits.

Catalytic Role of Thermostable Metalloproteases from Bacillus subtilis KT004404 as Dehairing and Destaining Agent

Crude oil biodegradation potential of biosurfactant-producing Pseudomonas aeruginosa and Meyerozyma sp.

A novel technique for interface analysis: Behaviour of sophorolipids biosurfactant obtained from Meyerozyma spp. MF138126 during low-salinity heavy-crude experiments

The distinctive chemical, physical, thermal and mechanical properties of graphene made it widely recognized material in wide-ranging field of science and technology. Generally, the synthesis of graphene or reduced graphene oxide (rGO) requires two main steps. The first step involves the oxidation of graphite to graphene oxide (GO) and in the second step, reducing agents or reductants contribute to the reduction of GO to form rGO. A large number of reducing agents have been applied to synthesize rGO such as hydrazine, hydroxyl amine, sodium borohydride, etc. However, the hazardous nature of such reducers created a space for the research on green reducing agents for rGO synthesis. This study introduces the low-cost green synthesis of rGO via green reducing agents such as eucalyptus hybrid extract, thiourea, lemon extract and starch. Among all the green reductants, eucalyptus hybrid extract exhibited the remarkable reduction of GO, as confirmed by VU-visible spectroscopy, Fourier transform infrared spectroscopy, and X-ray diffraction results. The absorption peak of rGO-eucalyptus is appeared at 272 nm, whereas the d-spacing between layers is determined to be 0.364 nm. The obtained band gap of rGO-eucalyptus (2 eV) is found less as compared with other reducing agents such as thiourea, lemon extract and starch. The stretching vibration of oxygen functionalities appeared in FTIR of GO, is disappeared after reduction with eucalyptus extract. The flavonoid components of eucalyptus extracts are antioxidant in nature and hence, work as reducing agents.

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Ramla Rehman

Papers

Current advances in the classification, production, properties and applications of microbial biosurfactants - A critical review.

Catalytic Role of Thermostable Metalloproteases from Bacillus subtilis KT004404 as Dehairing and Destaining Agent

Crude oil biodegradation potential of biosurfactant-producing Pseudomonas aeruginosa and Meyerozyma sp.

A novel technique for interface analysis: Behaviour of sophorolipids biosurfactant obtained from Meyerozyma spp. MF138126 during low-salinity heavy-crude experiments

Green synthesis and characterization of reduced graphene oxide