Evidence map›Paper›PMID 42793149›Full record

ReviewBiomolecules2026

Microbial Proteases as Product-Directed Catalysts for Industrial Proteolysis.

Sang-Woo Han

Abstract readReview
In one paragraph

Review in Biomolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

1 author.

Sang-Woo HanDepartment of Biotechnology, College of Biomedical & Health Science, Konkuk University, Chungju 27478, Chungbuk, Republic of Korea.ORCID 0000-0001-8708-3053

Funding

Konkuk University
6 · The paper itself

Abstract

Microbial proteases are widely used for industrial proteolysis in detergents, food processing, hydrolysate production, product stabilization, and side-stream valorization. Their industrial value is not determined by general activity or degree of hydrolysis alone, but by the ability of a defined catalyst to operate reliably under process conditions and generate the intended product endpoint. This review frames microbial proteases as product-directed biocatalysts whose performance depends on the alignment of catalyst identity, process compatibility, substrate access, and product outcome. Production, maturation, and immobilization are considered determinants of the deployed enzyme form, while biocatalyst identity, process translation, product outcome, and endpoint refinement provide a framework for evaluation. Across protease classes, industrial utility is shaped by acid-window matching, operating-window engineering, catalyst definition, metal-state compatibility, and peptide-pool refinement. Data-guided workflows integrating protease discovery and engineering, cleavage prediction, peptidomic mapping, real-substrate validation, and enzyme-system optimization offer a path toward more predictable product-oriented industrial proteolysis.

Indexed as

BacteriaPeptide HydrolasesProteolysisBiocatalysisProtein EngineeringPeptide Hydrolasesmicrobial proteasepeptide-pool remodelingproduct-oriented proteolysisprogrammable proteolysisprotease engineering

Identifiers

PMID42793149
PMCPMC13604415

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.