full issue - Association of Biotechnology and Pharmacy
full issue - Association of Biotechnology and Pharmacy
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