Quantitative Analysis of The High-Yield Hydrolysis of Kelp by Laminarinase and Alginate Lyase.

Autor: Takasuka TE; Research Faculty of Agriculture and, Graduate School of Global Food Resources, Hokkaido University, Sapporo, Japan.; Global Station for Food, Land and Water Resources, Hokkaido University, Sapporo, Japan.; US Department of Energy, Great Lakes Bioenergy Research Center, Madison, WI 53726, USA.; Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA., Kim H; US Department of Energy, Great Lakes Bioenergy Research Center, Madison, WI 53726, USA.; Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.; Present address: U.S. Department of Agriculture, Forest Service, Forest Products Laboratory, 1 Gifford Pinchot Drive, Madison, WI 53726, USA., Deng K; Department of Biomaterials and Biomanufacturing, Sandia National Laboratories, Livermore, CA 94551, USA.; US Department of Energy Joint BioEnergy Institute, Emeryville, CA94608, USA., Bianchetti CM; US Department of Energy, Great Lakes Bioenergy Research Center, Madison, WI 53726, USA.; Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA., Yamashita K; Research Faculty of Agriculture and, Graduate School of Global Food Resources, Hokkaido University, Sapporo, Japan., Beebe ET; US Department of Energy, Great Lakes Bioenergy Research Center, Madison, WI 53726, USA., Bergeman LF; US Department of Energy, Great Lakes Bioenergy Research Center, Madison, WI 53726, USA., Vander Meulen KA; US Department of Energy, Great Lakes Bioenergy Research Center, Madison, WI 53726, USA., Deutsch S; Department of Biomaterials and Biomanufacturing, Sandia National Laboratories, Livermore, CA 94551, USA., Ralph J; US Department of Energy, Great Lakes Bioenergy Research Center, Madison, WI 53726, USA.; Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA., Adams PD; US Department of Energy Joint BioEnergy Institute, Emeryville, CA94608, USA.; Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.; Department of Bioengineering, University of California, Berkeley, CA 94720, USA., Northen TR; US Department of Energy Joint BioEnergy Institute, Emeryville, CA94608, USA.; Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA., Fox BG; Global Station for Food, Land and Water Resources, Hokkaido University, Sapporo, Japan.; US Department of Energy, Great Lakes Bioenergy Research Center, Madison, WI 53726, USA.; Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2023 Oct 17; Vol. 24 (20), pp. e202300357. Date of Electronic Publication: 2023 Aug 28.
DOI: 10.1002/cbic.202300357
Abstrakt: Kelp is an abundant, farmable biomass-containing laminarin and alginate as major polysaccharides, providing an excellent model substrate to study their deconstruction by simple enzyme mixtures. Our previous study showed strong reactivity of the glycoside hydrolase family 55 during hydrolysis of purified laminarin, raising the question of its reactivity with intact kelp. In this study, we determined that a combination of a single glycoside hydrolase family 55 β-1,3-exoglucanase with a broad-specificity alginate lyase from the polysaccharide lyase family 18 gives efficient hydrolysis of untreated kelp to a mixture of simple sugars, that is, glucose, gentiobiose, mannitol-end glucose, and mannuronic and guluronic acids and their soluble oligomers. Quantitative assignments from nanostructure initiator mass spectrometry (NIMS) and 2D HSQC NMR spectroscopy and analysis of the reaction time-course are provided. The data suggest that binary combinations of enzymes targeted to the unique polysaccharide composition of marine biomass are sufficient to deconstruct kelp into soluble sugars for microbial fermentation.
(© 2023 The Authors. ChemBioChem published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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