A review on microbial proteases

Research Journal of Biotechnology

The use of enzymes in applied biotechnology has progressively increased in both industrial processes, products and in medical field. Proteolytic enzymes play an important regulatory role in many physiological processes and also represent a therapeutic target for several diseases including cancer, hypertension, blood clotting disorders, respiratory and viral infection. Proteases, a largest and ubiquitous class of enzymes, have a divergent role in biomedical field. The current review includes the basic information about the protease classification and optimized growth parameters to maximize the production of alkaline proteases and applications of proteases in a wide variety of industries including leather, textile, food manufacturing, pharmaceutical, detergent and waste management. The review also implicates the importance of genetic tools to obtain the novel engineered protease with improved catalytic performance and stability, pH and thermal tolerance.

Microorganisms are attractive sources of proteases as they can be artificially cultured in large quantities in a relatively short time by established fermentation methods. Microbial proteases have been and will continue to gain global significant prominence, particularly in commercial industries. Microbial alkaline proteases dominates the world enzyme market, accounting for a nearly two-thirds share of the detergent industry. Screening and characterization of these proteases from different sources serves many advantages from both environmental and industrial points of view. Most of the microbial proteases of significant application in detergent industry are bacterial alkaline proteases from genus Bacillus. The major bottleneck has been the screening of wild-type biocatalyst that would be detergent compatible with increase efficiency than what is seen today. Given their role in commercial industries; it is deemed imperative to gather the disperse literature on the current state of the art describing the sources, classification, application and biosynthetic regulation of bacterial proteases. Special emphasis has been given to bacterial alkaline proteases that are detergent compatible.

2016

Proteases catalyze hydrolysis of peptide bonds in proteins and are one of the most widely used industrial enzymes. Though they are ubiquitously found in a wide diversity of sources such as plants, animals, and microorganisms but microbial sources are preferred for the production of proteases due to technical and economic advantages. Microbial proteases have potential for application in different industries including detergent, leather, silver recovery, dairy, baking, beverages and pharmaceutical industries. These hydrolytic enzymes are efficiently involved in food industry for enhancing nutritional value, digestibility, palatability, flavour and reducing allergenic compounds as well as in management of domestic and industrial wastes. Furthermore, they are also involved in synthesis and structural elucidation of proteins. The present communication is an overview of the proteases produced from bacterial and fungal sources and their role in various industrial applications. Keyword: Pro...

The review briefly elucidates the importance of proteases in living organisms and their wide range of potential applications in the vast areas of research and biotechnology. The important features of the proteases are also exploited in a number of ways and can be used to serve various applications in different industries. Apart from their natural potential of performing various important operations in living tissues, various microbial proteases have potential applications in a number of industries. In cellular environment, proteases are involved in the breakdown of the proteins' peptide bonds and transform them into smaller fragments of amino acids and peptides which are prerequisite for the differentiation and cellular growth. Proteases have also vast applications in a range of industrial procedures such as food, pharmaceutical, dairy and detergent. Microbial proteases have dominated roles in the industrial sectors. Microbial proteases are exploited for their characteristic feature of hydrolyzing the protein and the rest of the components of wheat and soy beans in the production of soy sauce. The production of proteases can be enhanced via substantiated fermentation methods. The variation in the composition of growth media such as changes in carbon and nitrogen ratio and some other features affecting microbial growth are significant in the evaluating the fermentation procedures. The production of microbial proteases is advantageous because they can be generated rapidly, their production is cost effective and the manipulation of microbial enzymes is quite easy. Proteolytic enzymes can be produced by either submerged fermentation (SmF) or solid state fermentation (SSF). But the latter is far more advantageous because it direct towards many potential benefits for the protease production. The review mainly focuses on the microbial protease production, their functional and structural aspects and the application of these proteolytic enzymes in different industries.

2019

Industrial enzymes are the key to success of bioprocesses. New and emerging applications of these enzymes have opened new vistas in field of their production methods immensely. The industrial technical enzymes used for detergent, pulp and paper manufacturing, have a largest segment with nearly half of market share. Amongst these enzymes the largest share has been held by alkaline proteases, hence being the most valuable commercial enzyme. Alkaline proteases find their applications in the detergent and leather industries and there is an ever increasing trend to develop eco-friendly technologies. The microbes are best source for protease production because of their rapid growth and the ease with which they can be genetically manipulated to produce new enzymes with desirably changed properties according to the need of respective industry. Pseudomonas is a gram-negative bacterium that predominantly produces alkaline proteolytic enzymes. Fungal alkaline proteases are advantageous because...

3 Biotech

Proteases are ubiquitous enzymes, having significant physiological roles in both synthesis and degradation. The use of microbial proteases in food fermentation is an age-old process, which is today being successfully employed in other industries with the advent of 'omics' era and innovations in genetic and protein engineering approaches. Proteases have found application in industries besides food, like leather, textiles, detergent, waste management, agriculture, animal husbandry, cosmetics, and pharmaceutics. With the rising demands and applications, researchers are exploring various approaches to discover, redesign, or artificially synthesize enzymes with better applicability in the industrial processes. These enzymes offer a sustainable and environmentally safer option, besides possessing economic and commercial value. Various bacterial and fungal proteases are already holding a commercially pivotal role in the industry. The current review summarizes the characteristics and types of proteases, microbial source, their current and prospective applications in various industries, and future challenges. Promoting these biocatalysts will prove significant in betterment of the modern world.

Food Materials Research, 2023

Proteases are among the most important classes of hydrolytic enzymes and occupy a key position due to their applicability in both physiological and commercial fields. They are essential constituents of all forms of life, including plants, animals, and microorganisms. However, microorganisms represent an attractive source for protease secretion due to their high productivity in a relatively short time and limited space requirements for cultivation, amongst others. Microbial proteases are produced by submerged or solid-state fermentation process during postexponential or stationary growth phase. The production of these biocatalysts by microbes is influenced by nutritional and physicochemical parameters. Downstream recovery of high-value enzyme products from culture supernatant using suitable techniques is imperative prior to further use of the biocatalysts. Immobilization of these enzymes in appropriate matrices permits reusability, reclamation, enhanced stability and cost-effectiveness of the biocatalysts. The catalytic properties of microbial proteases help in the discovery of enzymes with high activity and stability, over extreme temperatures and pH for utilization in large-scale bioprocesses. This review provides insights into microbial proteases taking cognizance of the bioprocess parameters influencing microbial proteases production coupled with methods employed for protease purification as well as the immobilization and biochemical properties of the biocatalysts for potential biotechnological applications.

Frontiers in Bioengineering and Biotechnology, 2019

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.