| Literature DB >> 27287535 |
Keisuke Motone1, Toshiyuki Takagi2, Yusuke Sasaki3, Kouichi Kuroda1, Mitsuyoshi Ueda4.
Abstract
Laminarin is the algal storage glucan and represents up to 35% of the dry weight of brown macroalgae. In this study, a novel laminarinase, Gly5M, was first found using focused proteome analysis of a laminarin-assimilating marine bacterium, Saccharophagus degradans, and the encoding gene was isolated. A Gly5M-displaying yeast strain was prepared with the cell surface display system using Saccharomyces cerevisiae. It showed a laminarin-degrading activity on the cell surface and caused the dominant accumulation of gentiobiose. The obtained gentiobiose was converted into glucose and could be assimilated by an Aspergillus aculeatus β-glucosidase (BG)-displaying yeast strain. When Gly5M- and BG-displaying yeasts were anaerobically cultivated together in fermentation medium containing 20g/L laminarin as a sole carbon source, the coculture system with the combination of optimized ratios of the 2 yeast strains directly produced 5.2g/L ethanol. This coculture system of the 2 engineered yeast strains would be a platform for the use of laminarin and contribute to the complete utilization of brown macroalgae.Entities:
Keywords: Cell surface engineering; Coculture; Ethanol; Laminarin; Macroalgae; Saccharomyces cerevisiae
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Year: 2016 PMID: 27287535 DOI: 10.1016/j.jbiotec.2016.06.002
Source DB: PubMed Journal: J Biotechnol ISSN: 0168-1656 Impact factor: 3.307