Abstract
Enzymes are proteins highly specific in their actions on substrates and serve as biocatalysts. They are produced by cells in order to accelerate both the rate and specificity of metabolic reactions. Microbial enzymes are known for their unique characteristics over other sources due to their easy production on a commercial scale and stability. Different microorganisms are known to produce various enzymes such as bacteria, fungi and actinomycetes which produce a variety of extra-cellular and endo-cellular enzymes. Some of these actinomycetes enzymes have been isolated from the culture filtrates or the mycelium, concentrated and purified. Others have only been demonstrated in the mycelium of the organism. However, the ability to produce a variety of enzymes may be an attractive phenomenon in these microorganisms since they are nutritionally quite versatile. Microbial L-glutaminase has recently gained more attention due to its anticancer properties, in addition to its use as a flavor enhancer in food industry by increasing the amount of glutamic acid content in the fermented food .
References
Chandrasekaran M. 1997. Industrial enzymes from marine microorganisms. J Mar Biotech., 5:86-89.
Chou CC, Yu RC, Tsai CT. 1993. Production of glutaminase by Actinomucor elegans, Actinomucor taiwanensis and Aspergillus oryzae. J Chinese Agric Chem Soc., 31:78-86.
Chou CC, Hwan CH. 1994. Effect of ethanol on the hydrolysis of protein and lipid during the ageing of a Chinese fermented soya bean curdsufu. J Sci Food Agric., 66(3):393-398.
Imada A, Igarasi S, Nakahama K and Isono M. 1973. Asparaginase and Glutaminase activities of microorganisms. J Gen Microbiol., 76:85-99.
Kashyap P, Sabu A, Pandey A, Szakacs G and Soccol CR. 2002. Extra-cellular L-glutaminase production by Zygosaccharomyces rouxii under solid-state fermentation. Process Biochem., 38(3):307-312.
Koibuchi K, Nagasaki H, Yuasa A, Kataoka J and Kitamoto K. 2000. Molecular cloning and characterization of a gene encoding glutaminase from Aspergillus oryzae. Appl Microbiol Biotechnol., 54(1):59-68.
Krishnakumar S, Alexis R, Rajan and Ravikumar S. 2011. Extracellular production of L-glutaminase by marine alkalophilic Streptomyces sp. SBU1 isolated from Cape Comorin coast. Ind J Geo-Marine Sci., 40(5):717-721.
Lazarus P, Panasci LC. 1986; Characterization of L-Threonine and L-glutamine transport in murine P388 leukaemia cells in vitro. Biochim Biophys Acta 856(3):488-495.
Moriguchi M, Sakai K, Tateyama R, Furuta Y and Wakayama M. 1994. Isolation and characterization of salt-tolerant glutaminase from marine Micrococcus luteus K-3. J Ferment Bioeng. 77(6):621-625.
Nakadai T, Nasuno S. 1989. Use of glutaminase for soy sauce made by Koji or a preparation of proteases from Aspergillus oryzae. J Ferment Bioeng., 67(3):158-162.
Ohshima M, Yamamoto T and Soda K. 1976b. Further characterization of glutaminase isozymes from Pseudomonas aeruginosa. Agri Biologi Chem. 40(11):2251-2256.
O`Mahony M and Ishi M. 1987. The umami taste concept: Implications for the dogma of four basic tastes in Umami. Marcel Dekker, New York. 75-93.
Prabhu GN, Chandrasekaran M. 1995. Polystyrene - an inert carrier for glutaminase production by marine Vibrio costicola under Solid state fermentation. World J Microbiol Biotechnol., 11(6):683-684.
Roberts J, Holcenberg JS and Dolowy WC. 1970. Antineoplastic activity of highly purified bacterial glutaminase. Nature 227:1136-1137.
Sabu A. 2003. Sources, properties and applications of microbial therapeutic enzymes. Ind J Biotechnol., 2(3):334-341.
Santana CF de, Pinto Kde V, Moreira LC and Lacerda AL. 1968. Action of swine kidney L-glutaminase on Ehrlich carcinoma. Rev Inst Antibiot. ; 8(1):105-107.
Schuegerl K, Brandes L, Dullau T, Holzhauer-Rieger K, Hotop S and Huebner U. 1991. Fermentation monitoring and control by on-line flow injection and liquid chromatography. Anal Chim Acta. ; 249(1):87-100.
Sivakumar K, Sahu MK, Manivel PR and Kannan L. 2006. Optimum conditions for L-glutaminase production by actinomycete strain isolated from estuarine fish, Chanos chanos. Ind J Exp Biol., 44(3):256-258.
Tachiki T, Yamada T, Mizuno K, Ueda M, Shiode J and Fukami H. 1998. γ-Glutamyl transfer reactions by glutaminase from Pseudomonas nitroreducens IFO 12694 and their application for the syntheses of theanine and γ-glutamylmethylamide. Biosci Biotechnol Biochem., 62:1279-1283.
Tambekar DH and Tambekar SD. 2011. Partial characterization and optimization of protease production from newly isolated Cohnella thermotolerans from Lonar Lake. Journal of Research in Biology. 1(4):292-298.
Tanaka S, Robinson EA, Appella E, Miller M, Ammon HL, Roberts J, Weber IT and Wlodawer A. 1988. Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasifrcans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi. J Biol Chem., 263:8583-8591.
Underkofler LA, Barton RR and Rennert SS. 1958. Production of microbial enzymes and their applications. Appl Microbiol., 6(3):212-221.
Wade HE, Robinson HK and Phillips BW. 1971. Asparaginase and glutaminase activities of bacteria. J Gene Microbiol. 69:299-312.
Waksman SA. 1950. The actinomycetes: nature, occurance and activities. Waverly press, Baltimore, U.S.A.
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