Chandrasekaran, M; Suresh, P V(Elsevier, June 23, 1998)
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Abstract:
A chitinolytic fungus, Beau6eria bassiana was isolated from marine sediment and significant process parameters influencing
chitinase production in solid state fermentation using wheat bran were optimised. The organism was strongly alkalophilic and
produced maximum chitinase at pH 9·20. The NaCl and colloidal chitin requirements varied with the type of moistening medium
used. Vegetative (mycelial) inoculum was more suitable than conidial inoculum for obtaining maximal enzyme yield. The addition
of phosphate and yeast extract resulted in enhancement of chitinase yield. After optimisation, the maximum enzyme yield was
246·6 units g 1 initial dry substrate (U gIDS 1). This is the first report of the production of chitinase from a marine fungus.
Chandrasekaran, M; Rajeev Kumar, S; Keerthi, T R; Sabu, A(Elsevier, September 27, 1999)
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Abstract:
Extracellular L-glutaminase production by Beau6eria sp., isolated from marine sediment, was observed during solid state
fermentation using polystyrene as an inert support. Maximal enzyme production (49.89 U:ml) occurred at pH 9.0, 27°C, in a
seawater based medium supplemented with L-glutamine (0.25% w:v) as substrate and D-glucose (0.5% w:v) as additional carbon
source, after 96 h of incubation. Enzyme production was growth associated. Results indicate scope for production of salt tolerant
L-glutaminase using this marine fungus
Chandrasekaran, M; Sreeja, Chellappan; Jasmin, C; Soorej, Basheer M; Elyas, K K; Sarita,G Bhat(Elsevier, October 17, 2005)
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Abstract:
Engyodontium album isolated from marine sediment produced protease, which was active at pH 11. Process parameters influencing the
production of alkaline protease by marine E. album was optimized. Particle size of <425 mm, 60% initial moisture content and incubation at 25 8C
for 120 h were optimal for protease production under solid state fermentation (SSF) using wheat bran. The organism has two optimal pH (5 and 10)
for maximal enzyme production. Sucrose as carbon source, ammonium hydrogen carbonate as additional inorganic nitrogen source and amino acid
leucine enhanced enzyme production during SSF. The protease was purified and partially characterized. A 16-fold purified enzyme was obtained
after ammonium sulphate precipitation and ion-exchange chromatography. Molecular weight of the purified enzyme protein was recorded
approximately 38 kDa by SDS-PAGE. The enzyme showed maximum activity at pH 11 and 60 8C. Activity at high temperature and high alkaline
pH suggests suitability of the enzyme for its application in detergent industry