Evidence map›Paper›PMID 38532149›Full record

ReviewWorld journal of microbiology & biotechnology2024

Advances in recombinant protease production: current state and perspectives.

Xiufang Liu, Mulin Lian, Mouming Zhao, Mingtao Huang

Abstract readReview
PubMed Publisher
In one paragraph

Review in World journal of microbiology & biotechnology, 2024. 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
6.2field-weighted citation impact, top 3% 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, 16 citations in OpenAlex.

  1. Iterative evolution ofSynthetic and systems biotechnology · 2026
    Article
  2. Review
  3. Article
  4. Electrophoretic Zymography of Protease Using Azocasein.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  5. Article
  6. Article
  7. 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

4 authors at 1 institution in 1 country.

Xiufang LiuSchool of Food Science and Engineering, South China University of Technology, Guangzhou, 510641, China.
Mulin LianSchool of Food Science and Engineering, South China University of Technology, Guangzhou, 510641, China.
Mouming ZhaoSchool of Food Science and Engineering, South China University of Technology, Guangzhou, 510641, China.
Mingtao HuangSchool of Food Science and Engineering, South China University of Technology, Guangzhou, 510641, China. huangmt@scut.edu.cn.
South China University of Technology · CN

Funding

Key Area Research and Development Program of Guangdong Province, China 2022B0202030001Science and Technology Program of Guangzhou, China SL2023A04J00778
6 · The paper itself

Abstract

Proteases, enzymes that catalyze the hydrolysis of peptide bonds in proteins, are important in the food industry, biotechnology, and medical fields. With increasing demand for proteases, there is a growing emphasis on enhancing their expression and production through microbial systems. However, proteases' native hosts often fall short in high-level expression and compatibility with downstream applications. As a result, the recombinant production of proteases has become a significant focus, offering a solution to these challenges. This review presents an overview of the current state of protease production in prokaryotic and eukaryotic expression systems, highlighting key findings and trends. In prokaryotic systems, the Bacillus spp. is the predominant host for proteinase expression. Yeasts are commonly used in eukaryotic systems. Recent advancements in protease engineering over the past five years, including rational design and directed evolution, are also highlighted. By exploring the progress in both expression systems and engineering techniques, this review provides a detailed understanding of the current landscape of recombinant protease research and its prospects for future advancements.

Indexed as

BacillusPeptide HydrolasesBiotechnologyEndopeptidasesRecombinant ProteinsYeastsEndopeptidasesPeptide HydrolasesRecombinant ProteinsExpression systemsGenetic engineeringHigh-throughput screeningProtease engineeringRecombinant proteases

Identifiers

PMID38532149
OpenAlexW4394764800

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.