Immobilization of Dextranase on Nano-Hydroxyapatite as a Recyclable Catalyst.

Yanshuai Ding,Hangtian Zu,Mingsheng Lyu,Hao Zhang,Cang Wang,Xuelian Wang,Shujun Wang,Dongxue Dong

doi:10.3390/ma14010130

Yanshuai Ding, Hangtian Zu + Show 6 more

Open Access

https://doi.org/10.3390/ma14010130

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Journal: Materials	Publication Date: Dec 30, 2020
Citations: 18	License type: CC BY 4.0

Affiliation: Jiangsu Ocean University, Anhui University

Abstract

The immobilization technology provides a potential pathway for enzyme recycling. Here, we evaluated the potential of using dextranase immobilized onto hydroxyapatite nanoparticles as a promising inorganic material. The optimal immobilization temperature, reaction time, and pH were determined to be 25 °C, 120 min, and pH 5, respectively. Dextranase could be loaded at 359.7 U/g. The immobilized dextranase was characterized by field emission gun-scanning electron microscope (FEG-SEM), X-ray diffraction (XRD), and Fourier-transformed infrared spectroscopy (FT-IR). The hydrolysis capacity of the immobilized enzyme was maintained at 71% at the 30th time of use. According to the constant temperature acceleration experiment, it was estimated that the immobilized dextranase could be stored for 99 days at 20 °C, indicating that the immobilized enzyme had good storage properties. Sodium chloride and sodium acetic did not desorb the immobilized dextranase. In contrast, dextranase was desorbed by sodium fluoride and sodium citrate. The hydrolysates were 79% oligosaccharides. The immobilized dextranase could significantly and thoroughly remove the dental plaque biofilm. Thus, immobilized dextranase has broad potential application in diverse fields in the future.

Highlights

Dextranase (1,6-α-D-glucan 6-glucanohydrolase; EC 3.2.1.11) hydrolyzes α1,6 glycosidic bond of dextran with broad application prospects in diverse industries [1,2,3], such as in the production of low molecular-weight medical dextran and in food processing, sugarcane factories, and the prevention and treatment of dental plaque biofilms [4,5,6].The development of dextranase-immobilization technology is expected to provide a promising technology for its reuse [7,8]
The reaction time was at least 2 h (Figure 1b), and 81% dextranase was immobilized on HA
We co4n. dCuocntecdlusaiosnysstematic study to evaluate the feasibility of immobilizing dextranase on HA nWaenocopnadrtuicclteesd

Summary

Introduction

Dextranase (1,6-α-D-glucan 6-glucanohydrolase; EC 3.2.1.11) hydrolyzes α1,6 glycosidic bond of dextran with broad application prospects in diverse industries [1,2,3], such as in the production of low molecular-weight medical dextran and in food processing, sugarcane factories, and the prevention and treatment of dental plaque biofilms [4,5,6].The development of dextranase-immobilization technology is expected to provide a promising technology for its reuse [7,8]. The feasibility of immobilizing dextranase on different support materials has been verified via physical adsorption, ion adsorption, encapsulation, and covalent adsorption. It remains a challenge to identify materials that provide the requirements of special characteristics for higher enzyme immobilization efficiency. The carrier material should have a relatively high specific surface area to enable immobilization of a large amount of enzyme [9,10]. From the immobilization of biocatalysts to the recovery of enzymes, the mechanical resistance and thermal stability of the scaffolds are important throughout the process [11]. Another important parameter to be evaluated during the fixation process is the diffusion rate of the substrate to the catalyst. The identification of suitable materials for different enzymes remains the focus of attention of the researchers [12,13]

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