Bostrycin, a novel coupling agent for protein immobilization and prevention of biomaterial-centered infection produced by Nigrospora sp. No. 407

• Published in: Enzyme and microbial technology 2012-05, Vol.50 (6-7), p.287-292
• Main Authors: Yang, Wen-Jen, Yang, Chih-Sheng, Huang, Chen-Ji, Chen, Ko-Shao, Lin, Shuen-Fuh
• Format: Article
• Language: English
• Subjects: Anthraquinones - chemistry; Anthraquinones - metabolism; Anthraquinones - pharmacology; Anti-Bacterial Agents - biosynthesis; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - pharmacology; Antibacterial agents; antibacterial properties; antibiotics; Ascomycota - enzymology; Bacteriostasis; Biotechnology - methods; Bostrycin; Clostridium botulinum - drug effects; Coupling agent; enzyme activity; Enzyme Stability; Enzymes; Enzymes, Immobilized - chemistry; Enzymes, Immobilized - metabolism; Fabrics; Glucose oxidase; Glucose Oxidase - chemistry; Glucose Oxidase - metabolism; Glutaraldehyde; Immobilization; Infection; microbial growth; Microbial Sensitivity Tests; Nigrospora; polyethyleneimine; polypropylene; polypropylenes; Polypropylenes - chemistry; Protein immobilization; Staphylococcus aureus - drug effects; Surface modification; Surface Properties; Textiles; Thermal stability
• ISSN: 0141-0229; 1879-0909
• DOI: 10.1016/j.enzmictec.2012.02.002

► Bostrycin is a promising coupling agent that can immobilize protein on a matrix. ► Bostrycin can cause a matrix to exhibit antibacterial property. ► Bostrycin-treated nonwoven PP fabric can replace the use of glutaraldedyde. ► Bostrycin immobilized matrix can be used for biomedical and public health purposes. Bostrycin, a red antibacterial agent with tetrahydroanthraquinone structure, has been isolated from Nigrospora sp. No. 407. This study investigated the potential antibacterial and multifunctional properties of matrixes through immobilization of bostrycin on their surface for immobilization of protein and prevention of bacterial growth. Bostrycin was immobilized on nonwoven polypropylene (PP) fabric by a technique using glutaraldehyde and polyethyleneimine for the activation of the surface. Glucose oxidase immobilized on bostrycin-treated nonwoven PP fabric showed high activity. The immobilization process improved thermal stability of the enzymes. During repeated assay for 30 cycles, the enzyme activity dropped to only 70% of the initial activity. Both bostrycin-treated nonwoven PP fabric sample and subsequently immobilized glucose oxidase sample on the surface also still exhibited a bacteriostatic effect. This is the first study to show that bostrycin is a promising coupling agent for surface modification on matrix and its potential applications in protein immobilization and biomaterial-centered infection.