Enzyme immobilization on α-1,3-glucan: development of flow reactor with fusion protein of α-1,3-glucan binding domains and histamine dehydrogenase
Author:
Affiliation:
1. Graduate School of Sciences and Engineering, Yamagata University
2. Department of Applied Chemistry, Faculty of Life Sciences, Ritsumeikan University
Publisher
Microbiology Research Foundation
Subject
Applied Microbiology and Biotechnology,Microbiology
Link
https://www.jstage.jst.go.jp/article/jgam/69/4/69_2023.04.002/_pdf
Reference19 articles.
1. Bolivar, J.M., Woodley, J.M., and Fernandez-Lafuente, R. (2022) Is enzyme immobilization a mature discipline? Some critical considerations to capitalize on the benefits of immobilization. Chem. Soc. Rev., 51, 6251-6290.
2. Datta, S., Christena, L.R., and Rajaram, Y.R. (2013) Enzyme immobilization: an overview on techniques and support materials. 3 Biotech, 3, 1-9.
3. Fujieda, N., Satoh, A., Tsuse, N., Kano, K., and Ikeda, T. (2004) 6-S-cysteinyl flavin mononucleotide-containing histamine dehydrogenase from Nocardioides simplex: molecular cloning, sequencing, overexpression, and characterization of redox centers of enzyme. Biochemistry, 43, 10800-10808.
4. Han, Q., Gong, W., Zhang, Z., Wang, L., Wang, B. et al. (2021) Orientated Immobilization of FAD-Dependent glucose dehydrogenase on electrode by carbohydrate-Binding Module Fusion for Efficient Glucose Assay. Int. J. Mol. Sci., 22, 5529.
5. Horaguchi, Y., Yano, S., Takamatsu, K., Otsuka, Y., Suyotha, W. et al. (2023) Nigero-oligosaccharide production by enzymatic hydrolysis from alkaline-pretreated α-1,3-glucan. J. Biosci. Bioeng., 135, 182-189.
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