ArticleScientific reports2016
Improved catalytic efficiency, thermophilicity, anti-salt and detergent tolerance of keratinase KerSMD by partially truncation of PPC domain.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Review
- Keratinases: microbial sources, mechanisms, and industrial applications in waste valorization.Frontiers in microbiology · 2026Review
- Identification and characterization of a versatile keratinase, KerZJ, from Stenotrophomonas sp. LMY.World journal of microbiology & biotechnology · 2023Article
- Expression of a Salt-Tolerant Pseudolysin in Yeast for Efficient Protein Hydrolysis under High-Salt Conditions.Biomolecules · 2022Article
- Microbial keratinase and the bio-economy: a three-decade meta-analysis of research exploit.AMB Express · 2021Article
- Article
- Structure, Application, and Biochemistry of Microbial Keratinases.Frontiers in microbiology · 2021Review
- Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications.Frontiers in microbiology · 2020Review
- The discovery of novel heat-stable keratinases from Meiothermus taiwanensis WR-220 and other extremophiles.Scientific reports · 2017Article
- Secretory expression and purification of Bacillus licheniformis keratinase in insect cells.PloS one · 2017Article
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4 authors.
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Abstract
The keratinase from Stenotrophomonas maltophilia (KerSMD) is known for its high activity and pH stability in keratin degradation. However, catalytic efficiency and detergent tolerability need to be improved in order to be used for industrial application. In this work, we obtained several keratinase variants with enhanced catalytic efficiency, thermophilicity, and anti-salt and detergent tolerability by partially truncating the PPC domain of KerSMD. The variants all showed improved catalytic efficiency to synthetic substrate AAPF, with the V355 variant having the highest kcat /Km value of 143.6 s(-1) mM(-1). The truncation of keratinase had little effect on alkaline stability but obviously decreased collagenase activity, developing its potential application in leather treatment. The variants V380, V370, and V355 were thermophilic, with a 1.7-fold enhancement of keratinlytic activity at 60 °C when compared to the wild type. The entire truncation of PPC domain obtained the variant V355 with improved tolerance to alkalinity, salt, chaotropic agents, and detergents. The V355 variant showed more than a 40% improvement in activity under 15% (w/v) NaCl or 4% (w/v) SDS solution, showing excellent stability under harsh washing and unhairing conditions. Our work investigated how protein engineering affects the function of PPC domain of KerSMD.
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