Cry3Aa*SpyCatcher Fusion Crystals Produced in Bacteria as Scaffolds for Multienzyme Coimmobilization
Publication in refereed journal


Times Cited
Altmetrics Information
.

Other information
AbstractThe production of Cry3Aa enzyme fusion crystals in Bacillus thuringiensis provides a direct method to immobilize individual enzymes and thereby improve their stability and recyclability. Nevertheless, many reactions require multiple enzymes to produce a desired product; thus a general strategy was developed to extend our Cry3Aa technology to multienzyme coimmobilization. Here, we report the direct production of particles comprising a modified Cry3Aa (Cry3Aa*) fused to SpyCatcher002 (Cry3Aa*SpyCat2) for coimmobilization of model enzymes MenF, MenD, and MenH associated with the biosynthesis of menaquinone. The resultant coimmobilized particles showed improved reaction rates compared to free enzymes presumably due to the higher local enzyme substrate concentrations and enhanced enzyme coupling made possible by colocalization. Furthermore, coimmobilization of these enzymes on Cry3Aa*SpyCat2 led to increased thermal stability and recyclability of the overall multienzyme system. These characteristics together with its overall simplicity of production highlight the benefits of Cry3Aa*SpyCat2 crystals as a platform for enzyme coimmobilization.
All Author(s) ListSun Q, Heater BS, Li TL, Ye WJ, Guo ZH, Chan MK
Journal nameBioconjugate Chemistry
Year2022
Month2
Volume Number33
Issue Number2
PublisherAMER CHEMICAL SOC
Pages386 - 396
ISSN1043-1802
LanguagesEnglish-United Kingdom
Web of Science Subject CategoriesBiochemical Research Methods;Biochemistry & Molecular Biology;Chemistry, Multidisciplinary;Chemistry, Organic;Biochemistry & Molecular Biology;Chemistry

Last updated on 2024-20-08 at 00:30