Evidence map›Paper›PMID 39496784›Full record

ArticleScientific reports2024

Molecular characterization and computational analysis of a highly specific L-glutaminase from a marine bacterium Bacillus australimaris NIOT30.

Nishanthika Thenmozhi Kulasekaran, Vanlalrovi, Lenin Subramanian, Jung-Kul Lee, Dharani Gopal, Jeya Marimuthu

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Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Nishanthika Thenmozhi KulasekaranMarine Biotechnology Division, National Institute of Ocean technology, Pallikaranai, Chennai, 600100, Tamilnadu, India.
VanlalroviDepartment of Chemical Engineering, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Lenin SubramanianMarine Biotechnology Division, National Institute of Ocean technology, Pallikaranai, Chennai, 600100, Tamilnadu, India.
Jung-Kul LeeDepartment of Chemical Engineering, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul, 05029, Republic of Korea.
Dharani GopalMarine Biotechnology Division, National Institute of Ocean technology, Pallikaranai, Chennai, 600100, Tamilnadu, India. dhara@niot.res.in.
Jeya MarimuthuMarine Biotechnology Division, National Institute of Ocean technology, Pallikaranai, Chennai, 600100, Tamilnadu, India. jeya.niot@gov.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An alkaline active L-glutaminase (BALG) producing bacterium was screened and identified from seamount sediment samples of the Arabian Sea. The isolate was confirmed to be Bacillus australimaris NIOT30 based on morphological characteristics and 16 S rRNA gene sequencing. The glutaminase gene, balg was PCR amplified, cloned and expressed in E. coli BL21 (DE3) host. The molecular weight of purified BALG was estimated to be 36 kDa and the enzyme showed a specific activity of 507 ± 27 Umg

Indexed as

BacillusGlutaminaseAmino Acid SequenceBacterial ProteinsCloning, MolecularEnzyme StabilityEscherichia coliGeologic SedimentsHydrogen-Ion ConcentrationKineticsModels, MolecularPhylogenyRNA, Ribosomal, 16SSubstrate SpecificityTemperatureBacterial ProteinsGlutaminaseRNA, Ribosomal, 16SBacillus australimarisCharacterizationL-GlutaminaseSedimentSpecificity

Identifiers

PMID39496784
PMCPMC11535052

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