Why Inspection Microbial enzymes

Enzymes are important due to their many useful properties. Their development, to a great extent,

has been possible due to the availability of microbial sources. Microorganisms are of much

attention because they can be produced economically and are amenable to genetic improvement.

Microbial enzymes have replaced many plant and animal enzymes. They have found application

in many industries including foods, beverages, pharmaceuticals, detergents, textiles, leather,

chemicals, biofuels, animal feed, personal care, pulp and paper, diagnostics, and therapy. New

molecular methods, including genomics and metagenomics, are being employed for the

discovery of new enzymes from microbes. The development of recombinant DNA technology

has had a major effect on production levels of enzymes and represent a way to overproduce

industrially important microbial, plant, and animal enzymes. It has been estimated that between

of the world enzyme market is supplied by recombinant enzymes. In addition, directed evolution

techniques have allowed design of enzyme specificities and better performance

Microbial Enzymes of Use in Industry

A large variety of microorganisms produce potent biocatalysts as enzymes which vary in their

microbial sources, chemical properties, and mechanisms. Usually, microbial enzymes catalyze

the reactions of hydrolysis, oxidation, or reduction. Microbial enzymes have different active site

motifs targeting diversified substrates. They may catalyze the reaction by completely different

mechanisms even when they belong to the same class. Microbial enzymes are mainly produced

by submerged fermentation and solid state fermentation. The enormous diversity of microbial

enzymes makes them an interesting group of products for application in many areas such as

agricultural, chemical industry, food processing industry, , such as industrial applications of a

group of industrially used microbial enzymes, such as carbohydrases, proteases and lipases ood
processes technologies the different enzymes viz., asparaginase, lactase, lipase, transglutaminase,

protease, and pectinase are employed widely for clarification, removing lactose, cheese ripening,

and meat tenderization. Similarly other enzymes such as phytase, complex of cellulose, and

xylanase are gaining importance in different food process technologies. In this chapter, we are

discussing the different microbial enzymes along with sources and their role and functions in

different food and beverages processes.

Advantage of enzymes in food and biotechnology and suggests the future trends and

applications. Selected strains of molds, bacteria, and yeasts are currently used as sources of

enzymes for food processing. Aspergillus oryzae, Aspergillus niger, and Bacillus subtilis are the

three most useful, well-known, and safe microbial sources for enzymes. Enzymes have great

utility in food processing. For example, the processing of common foods such as bread, beer,

cheese, and soft drinks requires microbial enzymes as an integral part of their manufacture.

There are several advantages of enzymes in food processing over alternative physical or

chemical manipulations. First, enzymes catalyze a specific action, avoiding potentially

undesirable side reactions resulting from less specific processing methods, second, the extremes

of pH or temperature necessary for chemical or physical treatments are avoided by using

enzymes and this minimizes the side reactions as well. Many of the enzymes used in

biotechnology are derived from microbial sources. Microbial enzymes are often used in analysis,

such as the clinical use of fungal glucose oxidase and bacterial catalase to measure blood glucose

to monitor the diabetic condition.

 L-asparaginases

*Depletion of L-asparagine from plasma by L-asparaginase results in inhibition of RNA and DNA synThe
enzyme L-aspariginase (L-asparagine amidohydrolase;

*-catalyzes the hydrolysis of L-asparagine to Laspartic acid and ammonia.thesis with the subsequent

blastic cell apoptosis L-asparagine which is essential for most malignan lymphoblastic cells but not for

normal celL

Disadvantage

enzyme selectively hydrolyzes the extracellular amino acid L-asparagine into L-aspartate and ammonia,

leading to nutritional deficiencies, protein synthesis inhibition, and ultimately death of lymphoblastic

cells by apoptosis. Currently, bacterial asparaginases are used for treatment purpose but offers

scepticism due to a number of toxicities, including thrombosis, pancreatitis, hyperglycemia, and

hepatotoxicity. Resistance towards bacterial asparaginase is another major disadvantage during cancer

management. This situation attracted attention of researchers towards alternative sources of L-

asparaginase