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Updated: Feb 6, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
Paste stability of different starch modified by fusing hexose oxidase/carbohydrate-binding module
Siyu Liu1, Xuemin Kang1, Li Guo1
1State Key Laboratory of Green Papermaking and Resource Recycling, Shandong Key Laboratory of Healthy Food Resources Exploration and Creation, School of Food Sciences and Engineering, Major Scientific Research Project for the Construction of State Key Lab, Qilu University of Technology (Shandong Academy of Sciences), Jinan, China.
Abstract:
The study constructed a fusion enzyme, G/HCA, by fusing hexose oxidase (HOX) with carbohydrate-binding module 20 (CBM20) and linking it to maltotetraose-forming amylase (G4-amylase) via a flexible linker. Corn, pea, and tapioca starch were modified using G/HCA and compared with sequential treatment using G4-amylase followed by HOX (GHA). SEM revealed that G/HCA caused more extensive erosion than GHA in corn and tapioca starches. XRD indicated higher susceptibility of A-type crystalline starch to G/HCA. XPS confirmed successful oxidation by the characteristic O=C-O peak (289.0 eV), and carbonyl content quantification demonstrated superior oxidation efficiency of G/HCA. Furthermore, G/HCA treatment enhanced shear-thinning stability and reduced final viscosity in corn and tapioca starches. Enzyme modification decreased gel strength for corn and pea starches but increased it for tapioca starch. This study demonstrates that G/HCA achieves efficient starch modification through synergistic catalytic effects, offering a novel strategy for environmentally friendly production of functional oxidized starch.
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