ArticleMicrobial biotechnology2016
Enhancement of the catalytic efficiency and thermostability of Stenotrophomonas sp. keratinase KerSMD by domain exchange with KerSMF.
Article in Microbial biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Article
- Genome Insight and factorial design to elucidate the regulation of the tryptophan-mediated IAA biosynthetic pathway in an endophyte.Scientific reports · 2026Article
- An update on thermostable keratinases for protein engineering against feather pollutants.Applied microbiology and biotechnology · 2025Review
- Current Understanding of Feather Keratin and Keratinase and Their Applications in Biotechnology.Biochemistry research international · 2025Review
- Enhancement of novel Endo-polygalacturonase expression in Rhodotorula mucilaginosa PY18: insights from mutagenesis and molecular docking.Microbial cell factories · 2023Article
- Identification and characterization of a versatile keratinase, KerZJ, from Stenotrophomonas sp. LMY.World journal of microbiology & biotechnology · 2023Article
- Structure prediction, docking studies and molecular cloning of novel Pichia kudriavzevii YK46 metalloprotease (MetPr) for improvement of feather waste biodegradation.Scientific reports · 2023Article
- Bacterial Communities and Diversity of Western Ghats Soil: A Study of a Biodiversity Hotspot.Current microbiology · 2023Article
- Valorization of Livestock Keratin Waste: Application in Agricultural Fields.International journal of environmental research and public health · 2022Review
- Feather-Degrading Bacillus cereus HD1: Genomic Analysis and Its Optimization for Keratinase Production and Feather Degradation.Current microbiology · 2022Article
- Perspectives on Converting Keratin-Containing Wastes Into Biofertilizers for Sustainable Agriculture.Frontiers in microbiology · 2022Review
- Keratinases as Versatile Enzymatic Tools for Sustainable Development.Biomolecules · 2021Review
- Molecular strategies to increase keratinase production in heterologous expression systems for industrial applications.Applied microbiology and biotechnology · 2021Review
- Microbial keratinase and the bio-economy: a three-decade meta-analysis of research exploit.AMB Express · 2021Article
- Enhancement of Activity and Thermostability of Keratinase FromFrontiers in bioengineering and biotechnology · 2021Article
- Structure, Application, and Biochemistry of Microbial Keratinases.Frontiers in microbiology · 2021Review
- Deletion and Randomization of Structurally Variable Regions inInternational journal of molecular sciences · 2020Article
- Enhanced extracellular recombinant keratinase activity inRSC advances · 2019Article
- Microbial Proteases Applications.Frontiers in bioengineering and biotechnology · 2019Review
- Progress in Microbial Degradation of Feather Waste.Frontiers in microbiology · 2019Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we enhanced the catalytic efficiency and thermostability of keratinase KerSMD by replacing its N/C-terminal domains with those from a homologous protease, KerSMF, to degrade feather waste. Replacement of the N-terminal domain generated a mutant protein with more than twofold increased catalytic activity towards casein. Replacement of the C-terminal domain obviously improved keratinolytic activity and increased the k(cat)/K(m) value on a synthetic peptide, succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, by 54.5%. Replacement of both the N- and C-terminal domains generated a more stable mutant protein, with a Tm value of 64.60 ± 0.65°C and a half-life of 244.6 ± 2 min at 60°C, while deletion of the C-terminal domain from KerSMD or KerSMF resulted in mutant proteins exhibiting high activity under mesophilic conditions. These findings indicate that the pre-peptidase C-terminal domain and N-propeptide are not only important for substrate specificity, correct folding and thermostability but also support the ability of the enzyme to convert feather waste into feed additives.
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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.