A putative D-lyxose isomerase from Dictyoglomus turgidum was purified with a specific activity of 19 U/mg for D-lyxose isomerization by heat treatment and affinity chromatography. The native enzyme was estimated as a 42 kDa dimer by gel-filtration chromatography. The activity of the enzyme was highest for D-lyxose, suggesting that it is a D-lyxose isomerase. The maximum activity of the enzyme was at pH 7.5 and 75°C in the presence of 0.5 mM Co(2+), with a half-life of 108 min, K(m) of 39 mM, and k(cat) of 3,570 1/min. The enzyme is the most thermostable D-lyxose isomerase among those characterized to date. It converted 500 g D-xylulose/l to 380 g D-lyxose/l after 2 h. This is the highest concentration and productivity of D-lyxose reported thus far.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1007/s10529-012-0874-y | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The Dose-Response Effect of Fluoride Exposure on the Gut Microbiome and Its Functional Pathways in Rats.
Metabolites
November 2023
Department of Environmental Health, Zhejiang Provincial Center for Disease Control and Prevention, Hangzhou 310051, China.
Metabolic activities within the gut microbiome are intimately linked to human health and disease, especially within the context of environmental exposure and its potential ramifications. Perturbations within this microbiome, termed "gut microbiome perturbations", have emerged as plausible intermediaries in the onset or exacerbation of diseases following environmental chemical exposures, with fluoride being a compound of particular concern. Despite the well-documented adverse impacts of excessive fluoride on various human physiological systems-ranging from skeletal to neurological-the nuanced dynamics between fluoride exposure, the gut microbiome, and the resulting dose-response relationship remains a scientific enigma.
View Article and Find Full Text PDFEngineering the thermostability of d-lyxose isomerase from via multiple computer-aided rational design for efficient synthesis of d-mannose.
Synth Syst Biotechnol
June 2023
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, China.
d-Mannose is an attractive functional sugar that exhibits many physiological benefits on human health. The demand for low-calorie sugars and sweeteners in foods are increasingly available on the market. Some sugar isomerases, such as d-lyxose isomerase (d-LIase), can achieve an isomerization reaction between d-mannose and d-fructose.
View Article and Find Full Text PDFBiochemical and Structural Characterisation of a Novel D-Lyxose Isomerase From the Hyperthermophilic Archaeon sp.
Front Bioeng Biotechnol
August 2021
The Henry Wellcome Building for Biocatalysis, Biosciences, College of Life and Environmental Sciences, University of Exeter, Exeter, United Kingdom.
A novel D-lyxose isomerase has been identified within the genome of a hyperthermophilic archaeon belonging to the species. The enzyme has been cloned and over-expressed in and biochemically characterised. This enzyme differs from other enzymes of this class in that it is highly specific for the substrate D-lyxose, showing less than 2% activity towards mannose and other substrates reported for lyxose isomerases.
View Article and Find Full Text PDFIdentification of a novel recombinant D-lyxose isomerase from Thermoprotei archaeon with high thermostable, weak-acid and nickel ion dependent properties.
Int J Biol Macromol
December 2020
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu 214122, China.
Recently, production of D-mannose becomes a hotspot owing to it exhibiting many physiological functions on people's health and wide applications in food and pharmaceutical field. The use of biological enzymes to production of D-mannose is of particular receiving considerable concerns due to it possessing many merits over chemical synthesis and plant extraction strategies. D-Lyxose isomerase (D-LIase) plays a pivotal role in preparation of D-mannose from d-fructose through isomerization reaction.
View Article and Find Full Text PDFCharacterization of a recombinant D-mannose-producing D-lyxose isomerase from Caldanaerobius polysaccharolyticus.
Enzyme Microb Technol
August 2020
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, 214122, China; International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu, 214122, China.
Recently, functional sugars, such as d-mannose, have attracted considerable attention due to their excellent physiological benefits for human health and wide applications in food and pharmaceutical industries. Therefore, d-mannose production using a sugar isomerase such as d-lyxose isomerase (d-LIase) has emerged as a research hotspot owing to its advantages over plant extraction and chemical synthesis methods. In this study, a putative d-LIase gene from Caldanaerobius polysaccharolyticus was cloned and expressed in Escherichia coli.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!