Evidence map›Paper›PMID 27275826›Full record

ArticleMarine drugs2016

Enzymatic Hydrolysis of Alginate to Produce Oligosaccharides by a New Purified Endo-Type Alginate Lyase.

Benwei Zhu, Meijuan Chen, Heng Yin, Yuguang Du, Limin Ning

Open access · goldAbstract read
In one paragraph

Article in Marine drugs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
12.0field-weighted citation impact, top 1% 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

29 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Characterization of a NaWorld journal of microbiology & biotechnology · 2025
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  15. Biochemical and computational study of an alginate lyase produced byIranian journal of basic medical sciences · 2020
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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

5 authors at 3 institutions in 1 country.

Benwei ZhuPreclinical Medicine College, Nanjing University of Chinese Medicine, Nanjing 210023, China. zhubenwei@njtech.edu.cn.
Meijuan ChenPreclinical Medicine College, Nanjing University of Chinese Medicine, Nanjing 210023, China. meijuanchen@126.com.
Heng YinDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China. yinheng@dicp.ac.cn.
Yuguang DuInstitute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China. ygdu@ipe.ac.cn.
Limin NingPreclinical Medicine College, Nanjing University of Chinese Medicine, Nanjing 210023, China. ninglimin2006@126.com.
Nanjing University of Chinese Medicine · CNDalian Institute of Chemical Physics · CNInstitute of Process Engineering · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymatic hydrolysis of sodium alginate to produce alginate oligosaccharides has drawn increasing attention due to its advantages of containing a wild reaction condition, excellent gel properties and specific products easy for purification. However, the efficient commercial enzyme tools are rarely available. A new alginate lyase with high activity (24,038 U/mg) has been purified from a newly isolated marine strain, Cellulophaga sp. NJ-1. The enzyme was most active at 50 °C and pH 8.0 and maintained stability at a broad pH range (6.0-10.0) and temperature below 40 °C. It had broad substrate specificity toward sodium alginate, heteropolymeric MG blocks (polyMG), homopolymeric M blocks (polyM) and homopolymeric G blocks (polyG), and possessed higher affinity toward polyG (15.63 mM) as well as polyMG (23.90 mM) than polyM (53.61 mM) and sodium alginate (27.21 mM). The TLC and MS spectroscopy analysis of degradation products suggested that it completely hydrolyzed sodium alginate into oligosaccharides of low degrees of polymerization (DPs). The excellent properties would make it a promising tool for full use of sodium alginate to produce oligosaccharides.

Indexed as

AlginatesBacteriaBacterial ProteinsGlucuronic AcidHexuronic AcidsHydrogen-Ion ConcentrationHydrolysisOligosaccharidesPolysaccharide-LyasesSubstrate SpecificityTemperatureAlginatesBacterial ProteinsGlucuronic AcidHexuronic AcidsOligosaccharidespoly(beta-D-mannuronate) lyasePolysaccharide-Lyasesalginate lyaseCellulophagaenzymatic hydrolysisoligosaccharides

Identifiers

PMID27275826
PMCPMC4926067
OpenAlexW2413232978

What OpenQuestion holds

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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.