Evidence map›Paper›PMID 41273538›Full record

ArticleMolecular biotechnology2026

A Sequence-Based Approach Reveals a Novel Family IV Lipolytic Enzyme in Cereibacter sphaeroides 2.4.1.

Ramdhan Putrasetya, Griselda Herman Natadiputri, Rika Indri Astuti, Aris Tri Wahyudi, Antonius Suwanto

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Article in Molecular biotechnology, 2026. 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

5 authors.

Ramdhan PutrasetyaDepartment of Biology, Faculty of Mathematics and Natural Science, IPB University, Kampus IPB Dramaga, Bogor, 16680, Indonesia.
Griselda Herman NatadiputriDepartment of Biology, Faculty of Mathematics and Natural Science, IPB University, Kampus IPB Dramaga, Bogor, 16680, Indonesia.
Rika Indri AstutiDepartment of Biology, Faculty of Mathematics and Natural Science, IPB University, Kampus IPB Dramaga, Bogor, 16680, Indonesia.
Aris Tri WahyudiDepartment of Biology, Faculty of Mathematics and Natural Science, IPB University, Kampus IPB Dramaga, Bogor, 16680, Indonesia.
Antonius SuwantoDepartment of Biology, Faculty of Mathematics and Natural Science, IPB University, Kampus IPB Dramaga, Bogor, 16680, Indonesia. antoniussuwanto@gmail.com.ORCID http://orcid.org/0000-0002-8765-1548

Funding

Kementerian Pendidikan, Kebudayaan, Riset, dan Teknologi 027/E5/PG.02.00.PL/2024
6 · The paper itself

Abstract

Bacterial lipases and esterases are central to lipid metabolism and biotechnology, yet they are underexplored in purple non-sulfur photosynthetic bacteria. To address this gap, we mined the genome of Cereibacter sphaeroides 2.4.1 by retrieving the sequences annotated by alpha beta hydrolase, esterase, and lipase from NCBI database. All sequences aligned to well-known of bacterial esterase or lipase and the higher identity was cloned and expressed in Escherichi coli. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) confirmed soluble expression of four proteins, with LipCs2 (26.4 kDa), LipCs3 (39.4 kDa), and LipCs9 (24.1 kDa) showing activity on tributyrin agar and preference for short-chain para-nitrophenyl esters. Although LipCs9 (314.11 ± 2.44 mM h

Indexed as

Bacterial ProteinsEsterasesLipaseRhodobacter sphaeroidesAmino Acid SequenceCloning, MolecularEscherichia coliLipolysisMolecular Docking SimulationPhylogenyRecombinant ProteinsSubstrate SpecificityBacterial ProteinsEsterasesLipaseRecombinant ProteinsBacterial lipolytic enzymeCereibacter sphaeroides 2.4.1Escherichia coliFunctional characterizationProtein structure modeling

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.