Evidence map›Paper›PMID 19346347›Full record

ArticleApplied and environmental microbiology2009

Characterization of Rhamnosidases from Lactobacillus plantarum and Lactobacillus acidophilus.

Jules Beekwilder, Daniela Marcozzi, Samuele Vecchi, Ric de Vos, Patrick Janssen, Christof Francke, Johan van Hylckama Vlieg, Robert D Hall

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

41 citing papers in PubMed, 101 citations in OpenAlex.

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  14. α-L-rhamnosidase: production, properties, and applications.World journal of microbiology & biotechnology · 2023
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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 1 country.

Jules BeekwilderPlant Research International, Wageningen, The Netherlands. jules.beekwilder@wur.nl
Daniela Marcozzi
Samuele Vecchi
Ric de Vos
Patrick Janssen
Christof Francke
Johan van Hylckama Vlieg
Robert D Hall
Nederlands Instituut Voor Zuivel Oonderzoek · NLCentre for BioSystems Genomics · NLRadboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactobacilli are known to use plant materials as a food source. Many such materials are rich in rhamnose-containing polyphenols, and thus it can be anticipated that lactobacilli will contain rhamnosidases. Therefore, genome sequences of food-grade lactobacilli were screened for putative rhamnosidases. In the genome of Lactobacillus plantarum, two putative rhamnosidase genes (ram1(Lp) and ram2(Lp)) were identified, while in Lactobacillus acidophilus, one rhamnosidase gene was found (ramA(La)). Gene products from all three genes were produced after introduction into Escherichia coli and were then tested for their enzymatic properties. Ram1(Lp), Ram2(Lp), and RamA(La) were able to efficiently hydrolyze rutin and other rutinosides, while RamA(La) was, in addition, able to cleave naringin, a neohesperidoside. Subsequently, the potential application of Lactobacillus rhamnosidases in food processing was investigated using a single matrix, tomato pulp. Recombinant Ram1(Lp) and RamA(La) enzymes were shown to remove the rhamnose from rutinosides in this material, but efficient conversion required adjustment of the tomato pulp to pH 6. The potential of Ram1(Lp) for fermentation of plant flavonoids was further investigated by expression in the food-grade bacterium Lactococcus lactis. This system was used for fermentation of tomato pulp, with the aim of improving the bioavailability of flavonoids in processed tomato products. While import of flavonoids into L. lactis appeared to be a limiting factor, rhamnose removal was confirmed, indicating that rhamnosidase-producing bacteria may find commercial application, depending on the technological properties of the strains and enzymes.

Indexed as

Bacterial ProteinsCloning, MolecularEnzyme StabilityEscherichia coliFlavanonesFlavonoidsGene ExpressionGene OrderGlycoside HydrolasesHydrogen-Ion ConcentrationKineticsLactiplantibacillus plantarumLactobacillus acidophilusPhylogenyRhamnoseRutinBacterial ProteinsFlavanonesFlavonoidsGlycoside HydrolasesnaringinRhamnoseRutin

Identifiers

PMID19346347
PMCPMC2687308
OpenAlexW2121394348

What OpenQuestion holds

Textmetadata
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.