Bright Singh, I S; Saramma, A V; Jayesh, P; Manjusha, K; Prem, Gopinath; Priyaja, P; Divya, Jose; Sreelakshmi, B(Springer, June 21, 2012)
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Abstract:
Vibrio sp. V26 isolated from mangrove
sediment showed 98 % similarity to 16S rRNA gene
of Vibrio cholerae, V. mimicus, V. albensis and uncultured
clones of Vibrio. Phenotypically also it resembled
both V. cholerae and V. mimicus.Serogrouping, virulence
associated gene profiling, hydrophobicity, and adherence
pattern clearly pointed towards the non—toxigenic
nature of Vibrio sp. V26. Purification and characterization
of the enzyme revealed that it was moderately
thermoactive, nonhemagglutinating alkaline metalloprotease
with a molecular mass of 32 kDa. The application
of alkaline protease from Vibrio sp. V26 (APV26) in sub
culturing cell lines (HEp-2, HeLa and RTG-2) and
dissociation of animal tissue (chick embryo) for primary
cell culture were investigated. The time required for
dissociation of cells as well as the viable cell yield
obtained by while administeringAPV26 and trypsin were
compared. Investigations revealed that the alkaline
protease of Vibrio sp. V26 has the potential to be used
in animal cell culture for subculturing cell lines and
dissociation of animal tissue for the development of
primary cell cultures, which has not been reported earlier
among metalloproteases of Vibrios.
Description:
Cytotechnology (2013) 65:199–212
DOI 10.1007/s10616-012-9472-z
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