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Updated: Jul 13, 2026
11:27
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Detergent alkaline proteases: enzymatic properties, genes, and crystal structures
Katsuhisa Saeki1, Katsuya Ozaki, Tohru Kobayashi
1Tochigi Research Laboratories of Kao Corporation, 2606 Akabane, Ichikai, Haga 321-3497, Japan. saeki.katsuhisa@kao.co.jp
Journal of Bioscience and Bioengineering
|July 17, 2007
Summary
Bacillus proteases enhance detergents. Researchers produced M-protease and KP-43, a novel oxidatively stable protease, for industrial applications.
Area of Science:
- Biochemistry
- Enzymology
- Microbial Biotechnology
Background:
- Subtilisin-like serine proteases from Bacillus species are widely utilized in industrial applications, especially in laundry and dishwashing detergents.
- These proteases belong to family A of the subtilase superfamily, which includes true subtilisins, high-alkaline proteases, and intracellular proteases.
Observation:
- Large-scale production of a high-alkaline protease (M-protease) from alkaliphilic Bacillus clausii KSM-K16 was achieved and integrated into laundry detergents.
- Industrial-scale production of KP-43, a novel alkaline protease from Bacillus sp. strain KSM-KP43, demonstrated resistance to chemical oxidants and surfactants.
Findings:
- KP-43 and related proteases represent a new clan of oxidatively stable proteases within subtilase family A.
- The study details the enzymatic properties, gene sequences, and crystal structures of M-protease, KP-43, and associated enzymes.
Implications:
- The development of M-protease and KP-43 offers enhanced enzymatic solutions for detergent formulations, improving cleaning efficacy.
- Understanding the structural and functional characteristics of these novel proteases facilitates the design of next-generation industrial enzymes.
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