Enzymatic characterization of a novel recombinant 1,3-α-3,6-anhydro-L-galactosidase specific for neoagarobiose hydrolysis into monosaccharides
Author:
Funder
Kyungpook National University
Publisher
Springer Science and Business Media LLC
Subject
Applied Microbiology and Biotechnology,General Medicine,Biotechnology
Link
https://link.springer.com/content/pdf/10.1007/s00253-021-11341-8.pdf
Reference53 articles.
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2. Alkotaini B, Han NS, Kim BS (2017) Fusion of agarase and neoagarobiose hydrolase for mono-sugar production from agar. Appl Microbiol Biotechnol 101(4):1573–1580. https://doi.org/10.1007/s00253-016-8011-9
3. An K, Shi X, Cui F, Cheng J, Liu N, Zhao X, Zhang XH (2018) Characterization and overexpression of a glycosyl hydrolase family 16 β-agarase YM01-1 from marine bacterium Catenovulum agarivorans YM01T. Protein Expr Purif 143:1–8. https://doi.org/10.1016/j.pep.2017.10.002
4. Ariga O, Okamoto N, Harimoto N, Nakasaki K (2014) Purification and characterization of α-neoagarooligosaccharide hydrolase from Cellvibrio sp. OA-2007. J Microbiol Biotechnol 24(1):48–51. https://doi.org/10.4014/jmb.1307.07018
5. Asghar S, Lee CR, Park JS, Chi WJ, Kang DK, Hong SK (2018) Identification and biochemical characterization of a novel cold-adapted 1,3-α-3,6-anhydro-L-galactosidase, Ahg786, from Gayadomonas joobiniege G7. Appl Microbiol Biotechnol 102(20):8855–8866. https://doi.org/10.1007/s00253-018-9277-x
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2. Extracellular production of a thermostable Cellvibrio endolytic β-agarase in Escherichia coli for agarose liquefaction;AMB Express;2023-05-05
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