Purification and Characterization of α-Mannosidase from Onion, Allium cepa.

IF 1.2 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Journal of applied glycoscience Pub Date : 2024-04-20 eCollection Date: 2024-01-01 DOI:10.5458/jag.jag.JAG-2023_0010
Yui Narita, Yota Tatara, Shigeki Hamada, Kaoru Kojima, Shuai Li, Takashi Yoshida
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引用次数: 0

Abstract

α-Mannosidase (ALMAN) extracted from onion (Allium cepa) was purified by column chromatography such as hydrophobic and gel filtration. ALMAN is an acidic α-mannosidase that exhibits maximum activity against pNP-α-Man at pH 4.0-5.0 at 50°C. Amino acid sequence analysis of ALMAN was consistent with α-mannosidase deduced from Allium cepa transcriptome analysis. The gene alman was amplified by PCR using mRNA extracted from onions, and a full-length gene of 3,054 bp encoding a protein of 1,018 amino acid residues was revealed. ALMAN is classified as Glycoside Hydrolase Family (GH) 38 and showed homology with other plant-derived α-mannosidases such as tomato and hot pepper.

洋葱(Allium cepa)中 α-甘露糖苷酶的纯化和特性。
从洋葱(Allium cepa)中提取的α-甘露糖苷酶(ALMAN)是通过疏水和凝胶过滤等柱层析方法纯化的。ALMAN 是一种酸性 α-甘露糖苷酶,在 pH 值为 4.0-5.0 和 50°C 时对 pNP-α-Man 的活性最高。ALMAN 的氨基酸序列分析与薤白转录组分析推导出的α-甘露糖苷酶一致。利用从洋葱中提取的 mRNA,通过 PCR 扩增了 ALMAN 基因,并发现了一个长达 3,054 bp 的全长基因,编码 1,018 个氨基酸残基的蛋白质。ALMAN 被归类为糖苷水解酶家族(GH)38,与番茄和辣椒等其他植物来源的 α-甘露糖苷酶存在同源性。
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来源期刊
Journal of applied glycoscience
Journal of applied glycoscience BIOCHEMISTRY & MOLECULAR BIOLOGY-
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