Microbial enzymes

Microbial enzymes are identified to play a central role as metabolic catalysts, leading to their usage in various productions and applications , the end usage market for industrial enzymes is tremendously wide-spread with frequent industrial profitable applications (Adrio, et al., 2005). Over 500 industrial products are being complete using enzymes (Kumar, and Singh, et al., 2013). The request for industrial enzymes is on a incessant rise driven by a growing necessity for maintainable solutions.

Microbes have helped and continue to serve as one of the major and useful sources of numerous enzymes (Demain, and Adrio, et al., 2008). Many industrial processes, including chemical synthesis for manufacture of chemicals and pharmaceuticals . Furthermore, enzymes can be designated genetically and chemically-modified to improve their main properties: stability, substrate specificity and specific activity (Johnson, et al., 2013).

L-Glutaminase (L-glutamine amidohydrolase EC 3. 5. 1. 2) is known for its use as enzyme from diverse sources differ greatly in their possessions such as anticancer activity, immunogenicity, cytotoxicity, activity at physiological circumstances, plasma clearance rate, substrate specificity, temperature, pH and salt tolerance etc., there is a incessant search for L-glutaminase with properties appropriate for its use as antileukemic and/or flavor enhancing agent which plays a important role in the cellular nitrogen metabolism of together prokaryotic and eukaryotic cells (Sivakumar, et al., 2006).

In recent years, L-glutaminase has been deliberate due to their sole biotechnological flexibility and their ability to catalyst a wide spectrum of bioconversion responses of flavour compounds, L-glutaminase can be resulting from plant as well as animal foundations, microbial enzymes are commonly used for industrial determinations (Prakash, et al., 2009).

Another significant application of L- glutaminase is in biosensors for monitoring glutamine stages in mammalian and hybridoma cell cultures without the essential of distinct measurement of glutamic acid, L Glutaminase is usually observed as a key enzyme that controls the wonderful taste of fermented foods such as soy sauces (CruzSoto, et al., 1994).

On an industrial scale, L-glutaminases are produced largely by Aspergillus and Trichoderma sp. (Balagurunathan, et al., 2010). From an industrial opinion of view, filamentous fungi are chiefly stimulating as producers of L-glutaminase because they excrete significantly greater quantities of glutaminolytic enzymes into an extra cellular culture medium than bacteria or yeasts, industrially significant enzymes have conventionally been produced by submerged fermentation (SMF), But in recent years, SSF processes have been progressively used for the production of these enzymes. Interesting fact in SSF which added renewed notice from researchers in assessment of its economic and engineering advantages are cheap agro-industrial residues (Khandeparkar, et al., 2006). L-glutaminase has involved much care with respect to proposed applications in together pharmaceuticals and food. A diversity of microorganisms, comprising bacteria, yeast, filamentous fungi and molds have been described to produce L glutaminase (Iyer and Singhal, et al., 2008) of which the greatest potent producers are fungi (Balagurunathan, et al., 2010). L-glutaminase has recognized attention as a therapeutic in inconsistency of cancer and HIV (Rajeev Kumar, et al., 2003).

Other term of L-glutaminase Phosphate-activated glutaminase PAG is measured to be a mitochondrial enzyme, while PAG activity has also been create in nuclei in mouse tissue (Campos-Sandoval, et al., 2007).

For the production of field chemicals like theanine by c-glutamyl transfer reactions and as a flavour garnish in food industry (Renu, et al., 2003), the use of L-glutaminase as a flavour- garnish agent in Chinese foods has substituted the usage of monosodium glutamate which performances as an allergen for individuals (Jeon, et al., 2009).

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