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

A rational design for trypsin-resistant improvement of Armillariella tabescens β-mannanase MAN47 based on molecular structure evaluation.

Journal of biotechnology - 20 Feb 2013

Li Yufeng, Hu Fengjuan, Wang Xuman, Cao Hong, Liu Daling, Yao Dongsheng

Abstract excerpt

Protease resistance of enzymes is required for the feed industry because of the presence of secretary proteases in the digestive tract. In this study, we report a rational method for protease-resistance improvement of enzymes based on molecular structure evaluation. The trypsin-resistance of β-mannanase MAN47 from Armillariella tabescens was investigated. Twelve tryptic sites within it were ordered by their...

Read the complete abstract on PubMed

Topics

Armillaria
Computational Biology
Drug Resistance, Fungal
Escherichia coli
Models, Molecular
Molecular Dynamics Simulation

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

Molecular Structure

Mutagenesis, Site-Directed

Mutation

Protein Engineering

Trypsin

beta-Mannosidase

Source

Identifiers

PMID: 23318568
DOI: 10.1016/j.jbiotec.2012.12.018

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

A rational design for trypsin-resistant improvement of Armillariella tabescens β-mannanase MAN47 based on molecular structure evaluation.PMID 23318568Read ↗

Rational design of a thermophilic β-mannanase fromBacillus subtilis TJ-102 to improve its thermostability.Semantic proximity Read ↗

Characterizing pH-dependent stability profile of endo-β-mannanase enzyme: an in silico approach.Semantic proximity Read ↗

Improving the kinetic stability of a hyperthermostable β-mannanase by a rationally combined strategy.Semantic proximity Read ↗

Improving the Catalytic Properties of Xylanase from Alteromones Macleadii H35 Through Sequence Analysis.Semantic proximity Read ↗

A Novel Strategy for Thermostability Improvement of Trypsin Based on N-Glycosylation within the Ω-Loop Region.Semantic proximity Read ↗

Structural and functional relationship of Cassia obtusifolia trypsin inhibitor to understand its digestive resistance against Pieris rapae.Semantic proximity Read ↗

Functional and structural investigation of a novel β-mannanase BaMan113A from Bacillus sp. N16-5.Semantic proximity Read ↗

Structural and biochemical analyses of β-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila involved in mucin degradation.Semantic proximity Read ↗

Identification and Mutation Analysis of Nonconserved Residues on the TIM-Barrel Surface of GH5_5 Cellulases for Catalytic Efficiency and Stability Improvement.Semantic proximity Read ↗

Semi-rational design in simultaneous improvement of thermostability and activity of β-1,3-glucanase from Alkalihalobacillus clausii KSMK16.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 ↗

Rational design of thermostability in bacterial 1,3-1,4-β-glucanases through spatial compartmentalization of mutational hotspots.Semantic proximity Read ↗

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