Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Single-site substitutions improve cold activity and increase thermostability of the dehairing alkaline protease (DHAP).

Bioscience, biotechnology, and biochemistry - 1 Dec 2016

Zhao Hong-Yan, Wu Li-Ying, Liu Gang, Feng Hong

Abstract excerpt

To engineer dehairing alkaline protease (DHAP) variants to improve cold activity and increase thermostability so these variants are suitable for the leather processing industry. Based on previous studies with bacterial alkaline proteases, double-site mutations (W106K/V149I and W106K/M124L) were introduced into the DHAP from Bacillus pumilus. Compared with the wild-type DHAP hydrolytic activity, the double-site...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Bacillus

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Endopeptidases

Share to Enzyme Stability

Share to Hydrolysis

Share to Kinetics

Share to Protein Conformation

Share to Temperature

Source

Identifiers

PMID: 27609316
DOI: 10.1080/09168451.2016.1230005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single-site substitutions improve cold activity and increase thermostability of the dehairing alkaline protease (DHAP).PMID 27609316Read ↗

Single amino acid mutation alters thermostability of the alkaline protease from Bacillus pumilus: thermodynamics and temperature dependence.Semantic proximity Read ↗

Improving the catalytic activity and stability of Bacillus alcalophilus serine protease BAPB92 by rational design.Semantic proximity Read ↗

Engineering of protease-resistant phytase from Penicillium sp.: high thermal stability, low optimal temperature and pH.Semantic proximity Read ↗

Surfactant-tolerance evolution of Bacillus clausii protease for enhancing activity and stability by reshaping the substrate access tunnel.Semantic proximity Read ↗

Enhancement of keratinolytic activity of a thermophilic subtilase by improving its autolysis resistance and thermostability under reducing conditions.Semantic proximity Read ↗

Improvement in organic solvent resistance and activity of metalloprotease by directed evolution.Semantic proximity Read ↗

Propeptide engineering of Aspergillus niger-derived aspartic protease PepA for enhanced catalytic activity.Semantic proximity Read ↗

Optimization of Mutation Sites in Bacillus Velezensis Serine Protease for Enhanced Acid and Thermal Stability in Animal Feed Applications.Semantic proximity Read ↗

Engineering of the Phytase YiAPPA to Improve Thermostability and Activity and Its Application Potential in Dephytinization of Food Ingredients.Semantic proximity Read ↗

Enhancing thermostabilization of a newly discovered α-amylase from Bacillus cereus GL96 by combining computer-aided directed evolution and site-directed mutagenesis.Semantic proximity Read ↗

Improved thermostability of an acidic xylanase from Aspergillus sulphureus by combined disulphide bridge introduction and proline residue substitution.Semantic proximity Read ↗

The overexpression of the SAPB of Bacillus pumilus CBS and mutated sapB-L31I/T33S/N99Y alkaline proteases in Bacillus subtilis DB430: new attractive properties for the mutant enzyme.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.