Identification and characterization of xyloglucan-degradation related α-1,2-l-fucosidase in Aspergillus oryzae

IF 2.3 4区 生物学 Q3 BIOTECHNOLOGY & APPLIED MICROBIOLOGY Journal of bioscience and bioengineering Pub Date : 2024-06-12 DOI:10.1016/j.jbiosc.2024.05.011
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Abstract

Xyloglucan in plant cell walls has complex side-chain structures; Aspergillus oryzae produces various enzymes to degrade and assimilate xyloglucan. In this study, we identified and characterized α-1,2-l-fucosidase (AfcA) which is involved in xyloglucan degradation in A. oryzae. AfcA expression was induced in the presence of xyloglucan oligosaccharides. AfcA showed specific activity toward α-(1→2)-linked l-fucopyranosyl residues attached to the side chains of xyloglucan oligosaccharides and milk oligosaccharides, but not toward α-(1→3)-, α-(1→4)-, and α-(1→6)-linked l-fucopyranosyl residues. As fucopyranosyl residues in the side chains of xyloglucan oligosaccharides prevent the degradation of xyloglucan oligosaccharides by isoprimeverose-producing oligoxyloglucan hydrolase and β-galactosidase, the cooperative action of AfcA, isoprimeverose-producing oligoxyloglucan hydrolase, and β-galactosidase play a key role in degrading fucosylated xyloglucan in A. oryzae.

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鉴定和表征黑曲霉中与木聚糖降解相关的 α-1,2-l-岩藻糖苷酶
植物细胞壁中的木聚糖具有复杂的侧链结构;黑曲霉产生多种酶来降解和同化木聚糖。在这项研究中,我们发现并鉴定了参与黑曲霉降解木聚糖的α-1,2-l-岩藻糖苷酶(AfcA)。AfcA 的表达是在木聚糖寡糖存在的情况下诱导的。AfcA 对连接在木聚糖低聚糖和牛奶低聚糖侧链上的α-(1→2)-连接的 l-岩藻吡喃糖基残基具有特异性活性,但对α-(1→3)-、α-(1→4)-和α-(1→6)-连接的 l-岩藻吡喃糖基残基没有特异性活性。由于木聚糖低聚糖侧链中的岩藻吡喃糖基残基阻碍了异丙基藜芦糖产生的低聚木糖水解酶和β-半乳糖苷酶对木聚糖低聚糖的降解、AfcA、异丙聚糖低聚半乳糖水解酶和β-半乳糖苷酶的协同作用在降解A.oryzae。
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来源期刊
Journal of bioscience and bioengineering
Journal of bioscience and bioengineering 生物-生物工程与应用微生物
CiteScore
5.90
自引率
3.60%
发文量
144
审稿时长
51 days
期刊介绍: The Journal of Bioscience and Bioengineering is a research journal publishing original full-length research papers, reviews, and Letters to the Editor. The Journal is devoted to the advancement and dissemination of knowledge concerning fermentation technology, biochemical engineering, food technology and microbiology.
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