Evidence map›Paper›PMID 35069502›Full record

ArticleFrontiers in microbiology2021

The Function of CBM32 in Alginate Lyase VxAly7B on the Activity on Both Soluble Sodium Alginate and Alginate Gel.

Luyao Tang, Enwen Guo, Lan Zhang, Ying Wang, Shan Gao, Mengmeng Bao, Feng Han, Wengong Yu

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
3.8field-weighted citation impact, top 8% 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

7 citing papers in PubMed, 17 citations in OpenAlex.

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  7. Effects of Module Truncation of a New Alginate Lyase VxAly7C from MarineInternational journal of molecular sciences · 2022
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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 2 institutions in 1 country.

Luyao TangSchool of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
Enwen GuoSchool of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
Lan ZhangSchool of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
Ying WangSchool of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
Shan GaoSchool of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
Mengmeng BaoSchool of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
Feng HanSchool of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
Wengong YuSchool of Medicine and Pharmacy, Ocean University of China, Qingdao, China.
Qingdao National Laboratory for Marine Science and Technology · CNOcean University of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Carbohydrate-binding modules (CBMs), as an important auxiliary module, play a key role in degrading soluble alginate by alginate lyase, but the function on alginate gel has not been elucidated. Recently, we reported alginate lyase VxAly7B containing a CBM32 and a polysaccharide lyase family 7 (PL7). To investigate the specific function of CBM32, we characterized the full-length alginate lyase VxAly7B (VxAly7B-FL) and truncated mutants VxAly7B-CM (PL7) and VxAly7B-CBM (CBM32). Both VxAly7B-FL and native VxAly7B can spontaneously cleavage between CBM32 and PL7. The substrate-binding capacity and activity of VxAly7B-CM to soluble alginate were 0.86- and 1.97-fold those of VxAly7B-FL, respectively. Moreover, CBM32 could accelerate the expansion and cleavage of alginate gel beads, and the degradation rate of VxAly7B-FL to alginate gel beads was threefold that of VxAly7B-CM. Results showed that CBM32 is not conducive to the degradation of soluble alginate by VxAly7B but is helpful for binding and degradation of insoluble alginate gel. This study provides new insights into the function of CBM32 on alginate gel, which may inspire the application strategy of CBMs in insoluble substrates.

Indexed as

alginate gelalginate lyasebinding capacitycarbohydrate-binding module (CBM)functioninsoluble substrate

Identifiers

PMID35069502
PMCPMC8776709
OpenAlexW4206627250

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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.