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Coimmobilization of β-Agarase and α-Neoagarobiose Hydrolase for Enhancing the Production of 3,6-Anhydro-l-galactose
- Wang, Qidong, Sun, Jianan, Liu, Zhen, Huang, Wencan, Xue, Changhu, Mao, Xiangzhao
- Journal of agricultural and food chemistry 2018 v.66 no.27 pp. 7087-7095
- Fourier transform infrared spectroscopy, beta-agarase, biocatalysts, chemical bonding, magnetism, mutagenesis, nanoparticles, thermal stability
- Here we report a simple and efficient method to produce 3,6-anhydro-l-galactose (l-AHG) and agarotriose (AO3) in one step by a multienzyme system with the coimmobilized β-agarase AgWH50B and α-neoagarobiose hydrolase K134D. K134D was obtained by AgaWH117 mutagenesis and showed improved thermal stability when immobilized via covalent bonds on functionalized magnetic nanoparticles. The obtained multienzyme biocatalyst was characterized by Fourier transform infrared spectroscopy (FTIR). Compared with free agarases, the coimmobilized agarases exhibited a relatively higher agarose-to-l-AHG conversion efficiency. The yield of l-AHG obtained with the coimmobilized agarases was 40.6%, which was 6.5% higher than that obtained with free agarases. After eight cycles, the multienzyme biocatalyst still preserved 46.4% of the initial activity. To the best of our knowledge, this is the first report where two different agarases were coimmobilized. These results demonstrated the feasibility of the new method to fabricate a new multienzyme system onto magnetic nanoparticles via covalent bonds to produce l-AHG.