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full issue - Association of Biotechnology and Pharmacy

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Current Trends in <strong>Biotechnology</strong> <strong>and</strong> <strong>Pharmacy</strong><br />

Vol. 7 (1) 518-526 January 2013, ISSN 0973-8916 (Print), 2230-7303 (Online)<br />

525<br />

<strong>of</strong> 48 h to study its effect on L-asparaginase<br />

production. The maximum enzyme production<br />

(5.6 U/ml) was observed with 1.2 (% w/v) as<br />

shown in Fig. 7. Further increase in L-<br />

asparaginase concentration resulted in the<br />

decrement <strong>of</strong> enzyme production.<br />

Discussions for isolation <strong>of</strong> Streptomyces<br />

species strain: The strain grows well on most<br />

<strong>of</strong> the media. The sporophores occurred as spiral<br />

spore chains. The aerial mycelium developed<br />

moderately to good on most <strong>of</strong> the media <strong>and</strong> is<br />

gray in colour. The vegetative <strong>of</strong> the mycelium<br />

white to gray is almost dependent on media. The<br />

strain is non-chromogenic without any<br />

characteristic diffusible pigment <strong>and</strong> it produces<br />

soluble pigment. The strain H 2<br />

S <strong>and</strong> Tyrosinase<br />

reactions are positive. It showed moderate<br />

diastatic activity <strong>and</strong> showed a good proteolytic<br />

activity by hydrolyzing casein <strong>and</strong> starch. This<br />

strain PW-A12 is capable <strong>of</strong> coagulating <strong>and</strong><br />

peptonizing the milk. It exhibits positive nitrate<br />

reduction. It grows well at 37 o C. It tolerated the<br />

pH levels 6.5-7.5 good growth. It exhibited good<br />

growth on glucose, sucrose, Inositol, D-mannitol,<br />

D-fructose, lactose, maltose <strong>and</strong> Galactose. It<br />

showed poor to moderate growth on L-arabinose,<br />

D-xylose <strong>and</strong> cellulose. It exhibited good<br />

antibacterial activity. It exhibited good growth on<br />

L-arginine, L-cysteine <strong>and</strong> potassium nitrate.<br />

Moderate growth is on L-asparagine, L-histidine,<br />

<strong>and</strong> L-valine containing medium. Poor growth is<br />

on tyrosine containing medium.<br />

Summary <strong>and</strong> Conclusion<br />

Enzymes used for therapeutic purposes,<br />

cover a wide range <strong>of</strong> disease <strong>and</strong> conditions<br />

viz. inborn errors <strong>of</strong> metabolism, cancer, blood<br />

clotting deficiency etc. L-Asparaginase<br />

(E.C.3.5.1.1, L-Asparagin Amido hydrolase) used<br />

alone or in combination with other drugs is finding<br />

increased success in the management <strong>of</strong><br />

childhood lymphoblastic leukaemia. Keeping the<br />

potential <strong>of</strong> this particular enzyme in cancer<br />

treatment, the present work is planned with 5<br />

different estuarine sediment samples, 20<br />

Actinomycetes strains were isolated. Among<br />

them 5 strains showing pink colour zones with<br />

high intensity were selected for the production<br />

<strong>of</strong> L-asparaginase. Out <strong>of</strong> 5 Actinomycetes<br />

strains PW-A12, 4th strain exhibited maximum<br />

L-asparaginase activity with a yield <strong>of</strong> 3.933 IU/<br />

ml for 24 hrs Submerged Fermentation time.<br />

Further, optimizations <strong>of</strong> parameters were<br />

conducted with the strain PW-A12, by<br />

consecutive evaluation method. Maximum<br />

enzyme production with a yield <strong>of</strong> 5.73 IU/ml was<br />

observed with 4% peptone at pH 7.5. Reduced<br />

enzyme production was observed (5.6 IU/ml)<br />

while using on Yeast extract concentration <strong>of</strong> 1.2<br />

gm / 100 ml <strong>and</strong> at a pH <strong>of</strong> 7.0. After optimization,<br />

the production <strong>of</strong> L-asparaginase increased by<br />

1.45 times. The results <strong>of</strong> the present study<br />

indicated a scope for exploring estuarine<br />

Actinomycetes as a source for extracellular L-<br />

asparaginase, an enzyme that has gained<br />

industrial <strong>and</strong> pharmaceutical significance.<br />

References<br />

1. Goodfellow, M. <strong>and</strong> Cross, J. (1973).<br />

Taxonomy <strong>and</strong> classification <strong>of</strong> the<br />

actinomycetes. In: G. Sykes <strong>and</strong> FA Skinner<br />

(eds.), Actinomycetes, Character-istics <strong>and</strong><br />

practical Importance. Academic Press,<br />

London <strong>and</strong> New York. 11-112.<br />

2. Verma, N., Kumar, K., Kaur, G. <strong>and</strong> An<strong>and</strong><br />

S. (2007). L-asparaginase: a promising<br />

chemotherapeutic agent. Crit. Rev.<br />

Biotechnol., 27(1): 45-62.<br />

3. Tek, C.B., Monica, S. <strong>and</strong> Nitya, N.S. (2007)<br />

“Microbial production <strong>of</strong> Flavours <strong>and</strong><br />

fragrances; Fats <strong>and</strong> oils; Dyes; Bioplastics<br />

(PHAs);<br />

Polysaccharides;<br />

Pharmacologically active substances from<br />

marine microbes; Anti-cancer agents <strong>and</strong><br />

Microbial biotransformation”, Applied<br />

Microbiology.<br />

4. Peter, J.D. (1972) L-Asparaginase<br />

production by Streptomyces griseus, Appl<br />

Microbiol, 23: 1163–1164.<br />

5. Dhevagi, P. <strong>and</strong> Poorani, E. (2006).<br />

Isolation <strong>and</strong> characterization <strong>of</strong> L-<br />

Rao et al

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