Manjusha, K; Dr.Saramma, A V(Cochin University of Science and Technology, July , 2011)
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Abstract:
The thesis presents a detailed account of the alkaline protease produced by Vibrio sp.(V26) a mangrove isolate,and the application of this enzyme in different fields.The protease producer strain was identified on the basis of biochemical characteristice,putative virulence traits and 16S rRNA gene sequencing.The purification and characterization of the protease has been carried out. Along with this, an attempt has been made to identifiy the protease gene. The physical parameters as well as the media components influencing protease production were optimized using Response Surfce Methodology(RSM).The scale up of the application of the protease from Vibrio sp.(V26) in the dissociation of cells in animal cell culture,in the recovery of silver from used X-ray films as well as an ingredient in commercial detergents were investigated.
Description:
Dept.of Marine Biology,Microbiology and Biochemistry,Cochin University of Science and Technology
Sailas, Benjamin; Dr.Ashok, Pandey(Cochin University of Science And Technology, June , 1997)
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Abstract:
Strain improvement is one of the major objectives for maximizing the
microbial production of industrially significant primary and secondary metabolites.
This goal can be achieved by judicious tuning of the organisms by monitoring its
growth parameters and optimizing adequate supply of micro and macro nutrients,
inducers, pH, temperature and other factors which control fermentation. Though C.
rugosa has been under extensive studies for lipases, maximum world production is
only 36 units. In fact, in India, enhanced production conditions for lipases have not
yet been initiated. C. rugosa has been cultivated in diverse environments like
liquid, semi-solid, solid—state and immobilized conditions, though major emphasis is
on SmF or suspension culture. Hence the present investigations mainly focused on
increasing the yield by adjusting the physico-chemical growth parameters and to
characterize the lipase isoforms secreted by C. rugosa in the culture medium.
Maximum possible improved methods were investigated to achieve these objectives.
Within this under-optimised background, enhancement of lipase production
and its characterization were investigated, employing modified liquid, semi-solid,
solid—state and immobilized fermentation strategies
Description:
Biotechnology Division Regional Research Laboratory Trivandrum
Beena, P S; Dr.Chandrasekaran,M; Dr.Sarita,Bhat G(Cochin University of Science & Technology, January , 2010)
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Abstract:
Marine fungi remain totally unexplored as a source of industrial enzyme
and prospective applications. Further tannase production by a marine organism has
so far not been established. The primary objective of this study included the
evaluation of the potential of Aspergillus awamori isolated from sea water as part
of an earlier study and available in the culture collection of the Microbial
technology laboratory for tannase production through different fermentation
methods, optimization of bioprocess variables by statistical methods, purification
and characterization of the enzyme, genetic study, and assessment of its potential applications.
Description:
Department of Biotechnology,
Cochin University of Science and Technology
Chandrasekaran, M; Manzur Ali, P P; Rekha Mol, K R; Sapna, K; Sarita,G Bhat(Springer, March 11, 2014)
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Abstract:
Protease inhibitors can be versatile tools mainly in the fields of medicine, agriculture and
food preservative applications. Fungi have been recognized as sources of protease inhibitors,
although there are only few such reports on mushrooms. This work reports the purification and
characterization of a trypsin inhibitor from the fruiting body of edible mushroom Pleurotus
floridanus (PfTI) and its effect on the activity of microbial proteases. The protease inhibitor was
purified up to 35-fold by DEAE-Sepharose ion exchange column, trypsin-Sepharose column and
Sephadex G100 column. The isoelectric point of the inhibitor was 4.4, and its molecular mass was
calculated as 37 kDa by SDS-PAGE and 38.3 kDa by MALDI-TOF. Inhibitory activity confirmation
was by dot-blot analysis and zymographic activity staining. The specificity of the inhibitor
toward trypsin was with Ki of 1.043×10−10 M. The inhibitor was thermostable up to 90 °C with
maximal stability at 30 °C, active over a pH range of 4–10 against proteases from Aspergillus
oryzae, Bacillus licheniformis, Bacillus sp. and Bacillus amyloliquefaciens. Results indicate the
possibility of utilization of protease inhibitor from P. floridanus against serine proteases
Description:
Appl Biochem Biotechnol (2014) 173:167–178
DOI 10.1007/s12010-014-0826-1