Evidence map›Paper›PMID 29922971›Full record

ArticleCurrent microbiology2018

Surface Display of Heterologous β-Galactosidase in Food-Grade Recombinant Lactococcus lactis.

Supeng Yin, Hongbin Zhu, Mengyu Shen, Gang Li, Shuguang Lu, Yan Zhao, Shuai Le, Yinling Tan, Yizhi Peng, Fuquan Hu and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Current microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Screening for New Surface Anchoring Domains forFrontiers in microbiology · 2019
    Article
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

11 authors at 1 institution in 1 country.

Supeng YinDepartment of Microbiology, Third Military Medical University (Army Medical University), Chongqing, China.
Hongbin ZhuDepartment of Microbiology, Third Military Medical University (Army Medical University), Chongqing, China.
Mengyu ShenDepartment of Microbiology, Third Military Medical University (Army Medical University), Chongqing, China.
Gang LiDepartment of Microbiology, Third Military Medical University (Army Medical University), Chongqing, China.
Shuguang LuDepartment of Microbiology, Third Military Medical University (Army Medical University), Chongqing, China.
Yan ZhaoDepartment of Microbiology, Third Military Medical University (Army Medical University), Chongqing, China.
Shuai LeDepartment of Microbiology, Third Military Medical University (Army Medical University), Chongqing, China.
Yinling TanDepartment of Microbiology, Third Military Medical University (Army Medical University), Chongqing, China.
Yizhi PengState Key Laboratory of Trauma, Burns, and Combined Injury, Institute of Burn Research, Southwest Hospital, Third Military Medical University (Army Medical University), Chongqing, China.
Fuquan HuDepartment of Microbiology, Third Military Medical University (Army Medical University), Chongqing, China.
Jing WangDepartment of Microbiology, Third Military Medical University (Army Medical University), Chongqing, China. wangjing2008@aliyun.com.ORCID http://orcid.org/0000-0001-8125-3875
Army Medical University · CN

Funding

National Natural Science Foundation of China 31201341Third Military Medical University Youth Science Foundation 2010XQN06
6 · The paper itself

Abstract

β-Galactosidase is an essential enzyme for the metabolism of lactose in human beings and has an important role in the treatment of lactose intolerance (LI). β-Galactosidase expressed by intestinal microflora, such as lactic acid bacteria (LAB), also alleviates LI. A promising approach to LI management is to exploit a food-grade LAB delivery system that can inhabit the human intestine and overproduce β-galactosidase. In this study, we constructed a food-grade β-galactosidase surface display delivery system and then integrated into the chromosome of Lactococcus lactis (L. lactis) NZ9000 using recombination. Western blot and immunofluorescence analyses confirmed that β-galactosidase was expressed on the cell surface of recombinant L. lactis stain NZ-SDL. The whole-cell biocatalyst exhibits V

Indexed as

Gene ExpressionAnimalsbeta-GalactosidaseBiocatalysisCell MembraneCloning, MolecularEnzyme ActivationFemaleFluorescent Antibody TechniqueGenetic EngineeringGenetic VectorsHydrolysisLactococcus lactisMiceProtein Transportbeta-Galactosidase

Identifiers

PMID29922971
OpenAlexW2809131951

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.