AIMC Topic: Enzyme Stability
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Machine Learning and Chemical Imaging to Elucidate Enzyme Immobilization for Biocatalysis.
Analytical chemistry
Aug 24, 2021
Biocatalysis has rapidly become an essential tool in the scientific and industrial communities for the development of efficient, safe, and sustainable chemical syntheses. Immobilization of the biocatalyst, typically an engineered enzyme, offers signi...
Enhancement of protein thermostability by three consecutive mutations using loop-walking method and machine learning.
Scientific reports
Jun 4, 2021
We developed a method to improve protein thermostability, "loop-walking method". Three consecutive positions in 12 loops of Burkholderia cepacia lipase were subjected to random mutagenesis to make 12 libraries. Screening allowed us to identify L7 as ...
Machine Learning
Burkholderia cepacia
Hydrolases
Mutagenesis, Site-Directed
Protein Engineering
Mutation
Kinetics
Molecular Dynamics Simulation
Computational Biology
Enzyme Stability
Hot Temperature
Escherichia coli
Plasmids
Proteins
Lipase
Polymerase Chain Reaction
Mutagenesis
Molecular Conformation
Computational approach for identification, characterization, three-dimensional structure modelling and machine learning-based thermostability prediction of xylanases from the genome of Aspergillus fumigatus.
Computational biology and chemistry
Feb 6, 2021
Identification of thermostable and alkaline xylanases from different fungal and bacterial species have gained an interest for the researchers because of its biotechnological relevance in many industries, such as pulp, paper, and bioethanol. In this s...
Construction of arming Yarrowia lipolytica surface-displaying soybean seed coat peroxidase for use as whole-cell biocatalyst.
Enzyme and microbial technology
Dec 20, 2019
Whole-cell biocatalysts could be used in wide-ranging applications. In this study, a new kind of whole-cell biocatalyst was successfully constructed by genetically immobilizing soybean seed coat peroxidase (SBP) on the cell surface of Yarrowia lipoly...
Machine Learning Applied to Predicting Microorganism Growth Temperatures and Enzyme Catalytic Optima.
ACS synthetic biology
Jun 7, 2019
Enzymes that catalyze chemical reactions at high temperatures are used for industrial biocatalysis, applications in molecular biology, and as highly evolvable starting points for protein engineering. The optimal growth temperature (OGT) of organisms ...
Optimization of the production of an extracellular and thermostable amylolytic enzyme by Thermus thermophilus HB8 and basic characterization.
Extremophiles : life under extreme conditions
Dec 19, 2017
The objective of this study was to determine the potential of Thermus thermophilus HB8 for accumulating a high level of extracellular, thermostable amylolytic enzyme. Initial production tests indicated clearly that only very low levels of amylolytic ...
Purification and characterization of a protease from the visceral mass of Mytella charruana and its evaluation to obtain antimicrobial peptides.
Food chemistry
Nov 14, 2017
This work describes purification of a protease from the visceral mass of the mussel Mytella charruana as well as evaluation of its ability to hydrolyze milk casein to generate antimicrobial peptides. The enzyme showed pI of 4.1 and a single polypepti...
A novel aspartic protease from Rhizomucor miehei expressed in Pichia pastoris and its application on meat tenderization and preparation of turtle peptides.
Food chemistry
Oct 23, 2017
A novel aspartic protease gene (RmproA) was cloned from the thermophilic fungus Rhizomucor miehei CAU432 and expressed in Pichia pastoris. The RmproA was successfully expressed in P. pastoris as an active extracellular protease. High protease activit...
Purification and biochemical properties of SDS-stable low molecular weight alkaline serine protease from Citrullus colocynthis.
Natural product research
Sep 1, 2015
A low molecular weight serine protease from seeds of Citrullus colocynthis was purified to electrophoretic homogeneity with high level of catalytic efficiency (22,945 M(-1) S(-1)). The enzyme was a monomer with molecular mass of 25 kDa estimated by S...
Rational Design of an Epoxide Hydrolase From Spatholobus Suberectus: Enhancing Catalytic Activity and Thermostability for Efficient (R)-Styrene Oxide Production.
Biotechnology journal
Jun 1, 2025
(R)-Styrene oxide is a high-value chiral intermediate in pharmaceutical and chemical industries, yet its enantioselective synthesis remains challenging. Here, we engineered an epoxide hydrolase from Spatholobus suberectus (SsEH) to address its limita...
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