ArticleJournal of biological research (Thessalonike, Greece)2018
Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) from
Article in Journal of biological research (Thessalonike, Greece), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
4 citing papers in PubMed, 30 citations in OpenAlex.
- Characterization of a novel thermostable alkaline lipase derived from a compost metagenomic library and its potential application in the detergent industry.Frontiers in microbiology · 2022Article
- Molecular Characterization of Novel Family IV and VIII Esterases from a Compost Metagenomic Library.Microorganisms · 2021Article
- A proposed update for the classification and description of bacterial lipolytic enzymes.PeerJ · 2019Article
- Correction to: Molecular, biochemical and kinetic analysis of a novel, thermostable lipase (LipSm) fromJournal of biological research (Thessalonike, Greece) · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMicrobial lipases catalyze a broad spectrum of reactions and are enzymes of considerable biotechnological interest. The focus of this study was the isolation of new lipase genes, intending to discover novel lipases whose products bear interesting biochemical and structural features and may have a potential to act as valuable biocatalysts in industrial applications.
resultsA novel lipase gene (
conclusionsThe phylogenetic analysis of LipSm suggests the establishment of a new bacterial lipase family (XVIII) with LipSm being its first characterized member. Furthermore, LipSm is alkaliphilic, thermostable and lacks the requirement for interfacial activation, when small substrates are used. These properties make LipSm a potential advantageous biocatalyst in industry and biotechnology.
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Registered trials
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.