A hybrid-immobilization method was developed to improve the long-term stability of laminaribiose phosphorylase immobilized on epoxy supports Sepabeads EC-EP/S. Entrapment in chitosan retained all of the enzyme activity depending on the amount of entrapped solid materials and increased half-life by a factor of 10-94.4 h. No enzyme activity loss was determined during 12 times reuse. The immobilization method is also applicable to sucrose phosphorylase immobilized on Sepabeads EC-EP/S. Up to 31.9 g/L laminaribiose were produced in bienzymatic batch experiments with reaction-integrated product separation by adsorption on zeolites.

Download full-text PDF

Source
http://dx.doi.org/10.1007/s00449-017-1797-8DOI Listing

Publication Analysis

Top Keywords

phosphorylase immobilized
8
sepabeads ec-ep/s
8
enzyme activity
8
chitosan-based hybrid
4
hybrid immobilization
4
immobilization bienzymatic
4
bienzymatic reactions
4
reactions application
4
application production
4
production laminaribiose
4

Similar Publications

Compartmentalized co-immobilization of cellulase and cellobiose phosphorylase within zeolitic imidazolate framework efficiently synthesizes 1-p-Glc: Glycosylation of FDG.

Int J Biol Macromol

December 2024

Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, Changchun 130012, China. Electronic address:

Enzymatic glycosylation is an efficient and biocompatible approach to enhance natural product bioavailability. Cellobiose phosphorylase, a novel glycosyltransferase, utilizes 1-phospho-glucose (1-p-Glc) as a glycosyl donor for regioselective glycosylation of various natural substrates. However, the high cost of 1-p-Glc limits the economic feasibility of the process.

View Article and Find Full Text PDF

Development of an immobilized Mycobacterium tuberculosis purine nucleoside phosphorylase platform for ligand fishing and inhibition assays.

J Pharm Biomed Anal

February 2025

BioCrom, Instituto de Química, Departamento de Química Orgânica, Universidade Federal Fluminense, Niterói 24020-141, Brazil. Electronic address:

Article Synopsis
  • Purine nucleoside phosphorylase from Mycobacterium tuberculosis (MtPNP) is essential in purine metabolism, making it a promising target for new tuberculosis therapies, and this study created a ligand screening system using immobilized MtPNP on magnetic particles.
  • The platform allows for effective activity monitoring and inhibitor recognition, achieving significant results from a proof-of-concept study with competitive inhibition, indicating its utility in drug discovery.
  • Key parameters for improving ligand fishing assays were optimized, showing a balance must be struck between maximizing ligand isolation and maintaining enzyme activity for efficient, high-throughput screening.
View Article and Find Full Text PDF

Enzyme immobilization into carrier materials has broad importance in biotechnology, yet understanding the catalysis of enzymes bound to solid surfaces remains challenging. Here, we explore surface effects on the catalysis of sucrose phosphorylase through a fusion protein approach. We immobilize the enzyme via a structurally rigid α-helical linker [EAK] of tunable spacer length due to the variable number of pentapeptide repeats used ( = 6, 14, 19).

View Article and Find Full Text PDF

Spatially sequential co-immobilization of phosphorylases in tiny environments and its application in the synthesis of glucosyl glycerol.

Int J Biol Macromol

November 2024

Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, PR China. Electronic address:

2-O-(α-d-glucopyranosyl)-sn-glycerol (2-αGG) has been applied in the food industry due to its numerous physiological benefits. The synthesis of 2-αGG can be achieved through a cascade catalytic reaction involving sucrose phosphorylase (SP) and 2-O-α-glucosylglycerol phosphorylase (GGP). However, the low substrate transfer rates between free enzymes have hindered the efficiency of 2-αGG synthesis.

View Article and Find Full Text PDF

The acylation of flavonoids serves as a means to alter their physicochemical properties, enhance their stability, and improve their bioactivity. Compared with natural flavonoid glycosides, the acylation of nonglycosylated flavonoids presents greater challenges since they contain fewer reactive sites. In this work, we propose an efficient strategy to solve this problem based on a first α-glucosylation step catalyzed by a sucrose phosphorylase, followed by acylation using a lipase.

View Article and Find Full Text PDF

Want 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!