Evidence map›Paper›PMID 31976122›Full record

ReviewFood science and biotechnology2020

Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase.

Dong-Ho Seo, Sang-Ho Yoo, Seung-Jun Choi, Young-Rok Kim, Cheon-Seok Park

Erratum issuedAbstract readReview
In one paragraph

Review in Food science and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Enzymatic Glycosylation ofBiomolecules · 2025
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Molecular Docking and Kinetic Studies of the A226N Mutant ofJournal of microbiology and biotechnology · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Dong-Ho Seo1Department of Food Science and Technology, College of Agriculture and Life Sciences, Jeonbuk National University, Jeonju, 54896 Republic of Korea.
Sang-Ho Yoo2Department of Food Science and Biotechnology, and Carbohydrate Bioproduct Research Center, Sejong University, Seoul, 05006 Republic of Korea.
Seung-Jun Choi3Department of Food Science and Technology, Seoul National University of Science and Technology, Seoul, 01811 Republic of Korea.
Young-Rok Kim4Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University, Yongin, 17104 Republic of Korea.
Cheon-Seok Park4Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University, Yongin, 17104 Republic of Korea.ORCID 0000-0002-6921-3034

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amylosucrase (AS; EC 2.4.1.4) is an enzyme that has great potential in the biotechnology and food industries, due to its multifunctional enzyme activities. It can synthesize α-1,4-glucans, like amylose, from sucrose as a sole substrate, but importantly, it can also utilize various other molecules as acceptors. In addition, AS produces sucrose isomers such as turanose and trehalulose. It also efficiently synthesizes modified starch with increased ratios of slow digestive starch and resistant starch, and glucosylated functional compounds with increased water solubility and stability. Furthermore, AS produces turnaose more efficiently than other carbohydrate-active enzymes. Amylose synthesized by AS forms microparticles and these can be utilized as biocompatible materials with various bio-applications, including drug delivery, chromatography, and bioanalytical sciences. This review not only compares the gene and enzyme characteristics of microbial AS, studied to date, but also focuses on the applications of AS in the biotechnology and food industries.

Indexed as

AmyloseAmylosucraseEnzymatically modified starchTransglycosylationTuranose

Identifiers

PMID31976122
PMCPMC6949346

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.