Evidence map›Paper›PMID 35931938›Full record

ArticleThe protein journal2022

Functional Characterization of Recombinant Endo-Levanase (LevBk) from Bacillus koreensis HL12 on Short-Chain Levan-Type Fructooligosaccharides Production.

Hataikarn Lekakarn, Benjarat Bunterngsook, Phuphiphat Jaikaew, Thanyanun Kuantum, Rungtiva Wansuksri, Verawat Champreda

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Article in The protein journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.1field-weighted citation impact, top 25% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 10 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Hataikarn LekakarnDepartment of Biotechnology, Faculty of Science and Technology, Rangsit Campus, Thammasat University, Pathum Thani, 12120, Thailand.
Benjarat BunterngsookEnzyme Technology Research Team, Biorefinery Technology and Bioproduct Research Group, National Center for Genetic Engineering and Biotechnology, 113 Thailand Science Park, Phahonyothin Road, Khlong Luang, Pathum Thani, 12120, Thailand. benjarat.bun@biotec.or.th.ORCID 0000-0002-6741-684X
Phuphiphat JaikaewDepartment of Biotechnology, Faculty of Science and Technology, Rangsit Campus, Thammasat University, Pathum Thani, 12120, Thailand.
Thanyanun KuantumDepartment of Biotechnology, Faculty of Science and Technology, Rangsit Campus, Thammasat University, Pathum Thani, 12120, Thailand.
Rungtiva WansuksriCassava and Starch Technology Research Team, Functional Ingredients and Food Innovation Research Group, National Center for Genetic Engineering and Biotechnology, Bangkok, 10900, Thailand.
Verawat ChampredaEnzyme Technology Research Team, Biorefinery Technology and Bioproduct Research Group, National Center for Genetic Engineering and Biotechnology, 113 Thailand Science Park, Phahonyothin Road, Khlong Luang, Pathum Thani, 12120, Thailand.
National Center for Genetic Engineering and Biotechnology · THThammasat University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Levan-type fructooligosaccharides (L-FOSs) are a prominent class of non-digestible oligosaccharides with potential as nutritional prebiotics. Endo-levanase, which randomly hydrolyzes β-(2,6)-linkages in fructans, is a promising enzyme for short-chain FOS production. In this work, a recombinant levanase (LevBk) from Bacillus koreensis strain HL12 was characterized. Soluble LevBk protein was produced in Escherichia coli BL21(DE3) system at 40 mg/L of culture medium. Based on sequence and structural analysis, LevBk was classified as a member of endo-levanase in GH32 family containing N-terminal substrate binding pocket and C-terminal β-sandwich domains. LevBk optimally worked at 45 °C, pH 6.0 with the specific activity of 2.43 U/mg. Based on enzymatic hydrolysis, short-chain L-FOSs with degree of polymerization (DP) of 2-4 were produced from hydrolysis of timothy grass levan under optimal conditions for 9-24 h. With its ability to produce L-FOSs with specific chain lengths, LevBk could be attractively applied for converting of levan containing material to high value-added sweetener in the biorefinery industry.

Indexed as

FructansHexosyltransferasesBacillusGlycoside HydrolasesOligosaccharidesFructansfructooligosaccharideGlycoside HydrolasesHexosyltransferaseslevanaseOligosaccharidesBiorefineryEnzymatic hydrolysisFructooligosaccharidesLevanaseSweetener

Identifiers

PMID35931938
OpenAlexW4289929999

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.