ArticleBMC biotechnology2018
Engineering Bacillus pumilus alkaline serine protease to increase its low-temperature proteolytic activity by directed evolution.
Article in BMC biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 63 citations in OpenAlex.
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- Computer-directed rational engineering of dioxygenase TcsAB for triclosan biodegradation under cold conditions.Applied and environmental microbiology · 2025Article
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- Current status and emerging frontiers in enzyme engineering: An industrial perspective.Heliyon · 2024Review
- Enzymes for production of whey protein hydrolysates and other value-added products.Applied microbiology and biotechnology · 2024Review
- Exploring the molecular mechanism of cold-adaption of an alkaline protease mutant by molecular dynamics simulations and residue interaction network.Protein science : a publication of the Protein Society · 2023Article
- Microbial-derived salt-tolerant proteases and their applications in high-salt traditional soybean fermented foods: a review.Bioresources and bioprocessing · 2023Review
- Tuning transcription factor DegU for developing extracellular protease overproducer in Bacillus pumilus.Microbial cell factories · 2023Article
- Immobilization of Penicillin G Acylase on Vinyl Sulfone-Agarose: An Unexpected Effect of the Ionic Strength on the Performance of the Immobilization Process.Molecules (Basel, Switzerland) · 2022Article
- Making the cut with protease engineering.Cell chemical biology · 2022Review
- Article
- Characterization of a Protease Hyper-Productive Mutant of Bacillus pumilus by Comparative Genomic and Transcriptomic Analysis.Current microbiology · 2020Article
- Adaptation, production, and biotechnological potential of cold-adapted proteases from psychrophiles and psychrotrophs: recent overview.Journal, genetic engineering & biotechnology · 2020Review
- A novel DNA methylation motif identified in Bacillus pumilus BA06 and possible roles in the regulation of gene expression.Applied microbiology and biotechnology · 2020Article
- Early Stage Adaptation of a Mesophilic Green Alga to Antarctica: Systematic Increases in Abundance of Enzymes and LEA Proteins.Molecular biology and evolution · 2020Article
- The Practical Potential of Bacilli and Their Enzymes for Industrial Production.Frontiers in microbiology · 2020Review
- Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications.Frontiers in microbiology · 2020Review
- Enhanced extracellular recombinant keratinase activity inRSC advances · 2019Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMesophilic alkaline serine proteases from various bacteria have been commercially applied in a range of industries owing to their high catalytic efficiency and wide substrate specificity. However, these proteases have an optimal catalytic temperature of approximately 50 °C, and their activity decreases significantly at low temperature. Therefore, to enhance their cold activity, it is necessary to improve the catalytic performance of these proteases at low temperature. The alkaline serine protease (DHAP) from Bacillus pumilus BA06 is a typical mesophilic enzyme, which has demonstrated great potential in various industrial applications. Here we attempted to improve the cold activity of DHAP via directed evolution.
resultsSeven variants (P9S, A1G/K27Q, A38V, A116T, T162I, S182R, and T243S) of DHAP from B. pumilus were obtained via directed evolution. The results showed that all of the variants had increased proteolytic activity at 15 °C towards both the casein and synthetic peptide substrates. With the exception of variant T243S, the thermostability of these variants did not decrease in comparison with the wild-type enzyme. Kinetic analysis indicated that the increase in catalytic efficiency was largely attributed to the increase in turnover number (k
conclusionsDirected evolution and site-directed mutagenesis were combined to engineer variants of the DHAP from B. pumilus. All of the variants exhibited an increase in hydrolytic efficiency at low temperature towards both of the substrates, casein and synthetic peptide, without any loss of thermostability compared with the wild-type. These data suggest that engineering low-temperature activity for a bacterial protease is not always associated with the loss of thermostability. Furthermore, our findings demonstrate that enhanced cold activity and thermostability could be integrated into a single variant.
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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.