Evidence map›Paper›PMID 25173693›Full record

ArticleApplied microbiology and biotechnology2015

Biochemical and structural characterization of a thermostable β-glucosidase from Halothermothrix orenii for galacto-oligosaccharide synthesis.

Noor Hassan, Thu-Ha Nguyen, Montira Intanon, Lokesh D Kori, Bharat K C Patel, Dietmar Haltrich, Christina Divne, Tien Chye Tan

Open access · hybridAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 72 citations in OpenAlex.

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  8. Release of Soybean Isoflavones by Using a β-Glucosidase from Alicyclobacillus herbarius.Chembiochem : a European journal of chemical biology · 2021
    Article
  9. Article
  10. Crystal structure of a GH1 β-glucosidase from Hamamotoa singularis.Protein science : a publication of the Protein Society · 2020
    Article
  11. Article
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  15. A novel β-glucosidase fromBiotechnology for biofuels · 2018
    Article
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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

8 authors at 3 institutions in 4 countries.

Noor HassanKTH Royal Institute of Technology, School of Biotechnology, Albanova University Center, Roslagstullsbacken 21, S-10691, Stockholm, Sweden.
Thu-Ha Nguyen
Montira Intanon
Lokesh D Kori
Bharat K C Patel
Dietmar Haltrich
Christina Divne
Tien Chye Tan
BOKU University · ATKTH Royal Institute of Technology · SEGriffith University · AU

Funding

Austrian Science Fund FWF P 24868
6 · The paper itself

Abstract

Lactose is a major disaccharide by-product from the dairy industries, and production of whey alone amounts to about 200 million tons globally each year. Thus, it is of particular interest to identify improved enzymatic processes for lactose utilization. Microbial β-glucosidases (BGL) with significant β-galactosidase (BGAL) activity can be used to convert lactose to glucose (Glc) and galactose (Gal), and most retaining BGLs also synthesize more complex sugars from the monosaccharides by transglycosylation, such as galacto-oligosaccharides (GOS), which are prebiotic compounds that stimulate growth of beneficial gut bacteria. In this work, a BGL from the thermophilic and halophilic bacterium Halothermothrix orenii, HoBGLA, was characterized biochemically and structurally. It is an unspecific β-glucosidase with mixed activities for different substrates and prominent activity with various galactosidases such as lactose. We show that HoBGLA is an attractive candidate for industrial lactose conversion based on its high activity and stability within a broad pH range (4.5-7.5), with maximal β-galactosidase activity at pH 6.0. The temperature optimum is in the range of 65-70 °C, and HoBGLA also shows excellent thermostability at this temperature range. The main GOS products from HoBGLA transgalactosylation are β-D-Galp-(1→6)-D-Lac (6GALA) and β-D-Galp-(1→3)-D-Lac (3GALA), indicating that D-lactose is a better galactosyl acceptor than either of the monosaccharides. To evaluate ligand binding and guide GOS modeling, crystal structures of HoBGLA were determined in complex with thiocellobiose, 2-deoxy-2-fluoro-D-glucose and glucose. The two major GOS products, 3GALA and 6GALA, were modeled in the substrate-binding cleft of wild-type HoBGLA and shown to be favorably accommodated.

Indexed as

beta-GlucosidaseClostridiumCrystallography, X-RayEnzyme StabilityGalactoseGlucoseHydrogen-Ion ConcentrationLactoseModels, MolecularOligosaccharidesProtein ConformationSubstrate SpecificityTemperaturebeta-GlucosidaseGalactoseGlucoseLactoseOligosaccharides

Identifiers

PMID25173693
PMCPMC4322223
OpenAlexW2018931215

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.