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dc.contributor.authorShirodkar, P.V.
dc.contributor.authorMuraleedharan, U.D.
dc.contributor.authorDamare, S.R.
dc.contributor.authorRaghukumar, S.
dc.date.accessioned2020-12-31
dc.date.accessioned2021-02-09T10:13:19Z
dc.date.available2020-05-10
dc.date.available2021-02-09T10:13:19Z
dc.date.issued2020
dc.identifier.citationMarine Biotechnology, vol.22(3); 2020; 403-410
dc.identifier.issn1436-2236
dc.identifier.otherhttps://doi.org/10.1007/s10126-020-09960-9
dc.identifier.urihttps://doi.org/10.1007/s10126-020-09960-9
dc.identifier.urihttp://drs.nio.org/drs/handle/2264/8503
dc.descriptionIF2019 - 2.798
dc.description.abstractHalophilic bacteria are well known to produce highly salt-tolerant enzymes that have unusual applications in biotechnology. Production of halophilic proteins is generally not expected in mesohaline microorganisms. Ulkenia sp. AH-2, a mesohaline, marine straminipilan thraustochytrid isolated from waters of a mangrove ecosystem, produces halophilic alpha-amylases. Four enzyme fractions, viz., A, B, C, and D, were obtained upon ammonium sulfate fractionation and gel filtration. These had a broad salinity tolerance ranging from 0 to 4 M NaCl, with an optimum at 3 M NaCl. Pools A, C, and D each resolved as a single band on PAGE and zymogram analysis, and the purified proteins were designated Amy a, Amy c, and Amy h. The major activity resided in "pool B", consisting of several amylases which could not be further resolved into pure fractions. Together, these had an optimum at 2 M NaCl. All the enzymes were stable to storage for 2 to 24 h at 4 °C in a range of salt concentrations and even showed enhanced activity following such incubations. True to halophilic enzymes, the complex of "pool B" amylases showed improved activity in the presence of a wide range of organic solvents at 20% concentration. These enzymes are of particular interest by virtue of their constitutive nature as well as production under culture conditions that do not require salinity beyond that of seawater.
dc.languageen
dc.publisherSpringer
dc.relation.ispartofMar Biotechnol
dc.relation.isreferencedbySCI
dc.rightsOnly the author version of the copright reserved papers uploaded. Contact drs@nio.org for any complaints regarding copyright violations
dc.titleA Mesohaline Thraustochytrid Produces Extremely Halophilic Alpha-Amylases
dc.typeJournal Article
dc.affiliation.authorDepartment of Biotechnology, Goa University, Taleigao Plateau, Goa, 403 206, India


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