Redesign of a novel D-allulose 3-epimerase from Staphylococcus aureus for thermostability and efficient biocatalytic production of D-allulose.

Bacterial Proteins / biosynthesis Carbohydrate Epimerases / biosynthesis Fructose / biosynthesis Hydrogen-Ion Concentration Kinetics Metabolic Engineering Staphylococcus aureus / enzymology Substrate Specificity
D-Allulose 3-epimerase Site-directed saturation mutagenesis Structural analysis TIM-barrel fold Thermostability

Journal

Microbial cell factories
ISSN: 1475-2859
Titre abrégé: Microb Cell Fact
Pays: England
ID NLM: 101139812

Informations de publication

Date de publication:
25 Mar 2019
Historique:
received: 03 01 2019
accepted: 18 03 2019
entrez: 27 3 2019
pubmed: 27 3 2019
medline: 18 7 2019
Statut: epublish

Résumé

A novel D-allulose 3-epimerase from Staphylococcus aureus (SaDAE) has been screened as a D-allulose 3-epimerase family enzyme based on its high specificity for D-allulose. It usually converts both D-fructose and D-tagatose to respectively D-allulose and D-sorbose. We targeted potential biocatalysts for the large-scale industrial production of rare sugars. SaDAE showed a high activity on D-allulose with an affinity of 41.5 mM and catalytic efficiency of 1.1 s We redesigned SaDAE for thermostability and biocatalytic production of D-allulose. The research will aid the development of industrial biocatalysts for D-allulose.

Sections du résumé

BACKGROUND BACKGROUND
A novel D-allulose 3-epimerase from Staphylococcus aureus (SaDAE) has been screened as a D-allulose 3-epimerase family enzyme based on its high specificity for D-allulose. It usually converts both D-fructose and D-tagatose to respectively D-allulose and D-sorbose. We targeted potential biocatalysts for the large-scale industrial production of rare sugars.
RESULTS RESULTS
SaDAE showed a high activity on D-allulose with an affinity of 41.5 mM and catalytic efficiency of 1.1 s
CONCLUSIONS CONCLUSIONS
We redesigned SaDAE for thermostability and biocatalytic production of D-allulose. The research will aid the development of industrial biocatalysts for D-allulose.

Identifiants

DOI: 10.1186/s12934-019-1107-z PMID: 30909913 PMC: PMC6432756
pubmed: 30909913
doi: 10.1186/s12934-019-1107-z
pii: 10.1186/s12934-019-1107-z
pmc: PMC6432756
doi:

Substances chimiques

Bacterial Proteins 0
psicose 23140-52-5
Fructose 30237-26-4
Carbohydrate Epimerases EC 5.1.3.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

59

Subventions

Organisme : National Natural Science Foundation of China
ID : 31771911

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Auteurs

Zhangliang Zhu (Z)

Key Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.

Dengke Gao (D)

Key Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.

Chao Li (C)

Key Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.

Ying Chen (Y)

Key Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.

Menglu Zhu (M)

Key Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.

Xin Liu (X)

Key Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.

Masaru Tanokura (M)

Key Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China. amtanok@mail.ecc.u-tokyo.ac.jp.
Laboratory of Basic Science on Healthy Longevity, Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo, Tokyo, 113-8657, Japan. amtanok@mail.ecc.u-tokyo.ac.jp.

Hui-Min Qin (HM)

Key Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China. huiminqin@tust.edu.cn.

Fuping Lu (F)

Key Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China. lfp@tust.edu.cn.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines bactériennes › Redesign of a novel D-allulose 3-epimerase...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Isomerases › Racémases et épimérases › Carbohydrate epimerases › Redesign of a novel D-allulose 3-epimerase...
questionsmedicales.fr › Glucides › Sucres › Oses › Cétoses (sucres) › Fructose › Redesign of a novel D-allulose 3-epimerase...
questionsmedicales.fr › Phénomènes chimiques › Concentration en ions d'hydrogène › Redesign of a novel D-allulose 3-epimerase...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Cinétique › Redesign of a novel D-allulose 3-epimerase...
questionsmedicales.fr › Technologie, industrie et agriculture › Ingénierie › Bioingénierie › Ingénierie cellulaire › Génie métabolique › Redesign of a novel D-allulose 3-epimerase...
questionsmedicales.fr › Bactéries › Bactéries à Gram positif › Cocci à Gram positif › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Redesign of a novel D-allulose 3-epimerase...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Spécificité du substrat › Redesign of a novel D-allulose 3-epimerase...