Characterization of a GH36 α-D-Galactosidase Associated with Assimilation of Gum Arabic in Bifidobacterium longum subsp. longum JCM7052.

IF 1.2 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Journal of applied glycoscience Pub Date : 2021-06-11 eCollection Date: 2021-01-01 DOI:10.5458/jag.jag.JAG-2021_0004
Yuki Sasaki, Yumi Uchimura, Kanefumi Kitahara, Kiyotaka Fujita
{"title":"Characterization of a GH36 α-D-Galactosidase Associated with Assimilation of Gum Arabic in <i>Bifidobacterium longum</i> subsp. <i>longum</i> JCM7052.","authors":"Yuki Sasaki,&nbsp;Yumi Uchimura,&nbsp;Kanefumi Kitahara,&nbsp;Kiyotaka Fujita","doi":"10.5458/jag.jag.JAG-2021_0004","DOIUrl":null,"url":null,"abstract":"<p><p>We recently characterized a 3-<i>O</i>-α-D-galactosyl-α-L-arabinofuranosidase (GAfase) for the release of α-D-Gal-(1→3)-L-Ara from gum arabic arabinogalactan protein (AGP) in <i>Bifidobacterium longum</i> subsp. <i>longum</i> JCM7052. In the present study, we cloned and characterized a neighboring α-galactosidase gene (BLGA_00330; <i>blAga3</i>). It contained an Open Reading Frame of 2151-bp nucleotides encoding 716 amino acids with an estimated molecular mass of 79,587 Da. Recombinant BlAga3 released galactose from α-D-Gal-(1→3)-L-Ara, but not from intact gum arabic AGP, and a little from the related oligosaccharides. The enzyme also showed the activity toward blood group B liner trisaccharide. The specific activity for α-D-Gal-(1→3)-L-Ara was 4.27- and 2.10-fold higher than those for melibiose and raffinose, respectively. The optimal pH and temperature were 6.0 and 50 °C, respectively. BlAga3 is an intracellular α-galactosidase that cleaves α-D-Gal-(1→3)-L-Ara produced by GAfase; it is also responsible for a series of gum arabic AGP degradation in <i>B. longum</i> JCM7052.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.2000,"publicationDate":"2021-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/27/a8/JAG-68-047.PMC8367640.pdf","citationCount":"5","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of applied glycoscience","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.5458/jag.jag.JAG-2021_0004","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2021/1/1 0:00:00","PubModel":"eCollection","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 5

Abstract

We recently characterized a 3-O-α-D-galactosyl-α-L-arabinofuranosidase (GAfase) for the release of α-D-Gal-(1→3)-L-Ara from gum arabic arabinogalactan protein (AGP) in Bifidobacterium longum subsp. longum JCM7052. In the present study, we cloned and characterized a neighboring α-galactosidase gene (BLGA_00330; blAga3). It contained an Open Reading Frame of 2151-bp nucleotides encoding 716 amino acids with an estimated molecular mass of 79,587 Da. Recombinant BlAga3 released galactose from α-D-Gal-(1→3)-L-Ara, but not from intact gum arabic AGP, and a little from the related oligosaccharides. The enzyme also showed the activity toward blood group B liner trisaccharide. The specific activity for α-D-Gal-(1→3)-L-Ara was 4.27- and 2.10-fold higher than those for melibiose and raffinose, respectively. The optimal pH and temperature were 6.0 and 50 °C, respectively. BlAga3 is an intracellular α-galactosidase that cleaves α-D-Gal-(1→3)-L-Ara produced by GAfase; it is also responsible for a series of gum arabic AGP degradation in B. longum JCM7052.

Abstract Image

Abstract Image

Abstract Image

与长双歧杆菌阿拉伯胶同化相关的GH36 α- d -半乳糖苷酶的鉴定longum JCM7052。
我们最近在长双歧杆菌亚种鉴定了一种3- o -α- d -半乳糖-α- l-阿拉伯糖醛酸苷酶(GAfase),用于从阿拉伯半乳糖胶蛋白(AGP)中释放α-D-Gal-(1→3)- l- ara。longum JCM7052。在本研究中,我们克隆并鉴定了相邻的α-半乳糖苷酶基因(BLGA_00330;blAga3)。它包含一个2151 bp核苷酸的开放阅读框,编码716个氨基酸,估计分子质量为79,587 Da。重组BlAga3从α-D-Gal-(1→3)- l- ara中释放半乳糖,但不从完整的阿拉伯胶AGP中释放半乳糖,从相关的低聚糖中释放少量半乳糖。该酶对血B型内胆三糖也有活性。α-D-Gal-(1→3)- l- ara的比活性分别比蜜二糖和棉子糖高4.27倍和2.10倍。最适pH为6.0℃,最适温度为50℃。BlAga3是一种细胞内α-半乳糖苷酶,可裂解由GAfase产生的α-D-Gal-(1→3)- l- ara;它还负责长叶树胶JCM7052中一系列阿拉伯树胶AGP的降解。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Journal of applied glycoscience
Journal of applied glycoscience BIOCHEMISTRY & MOLECULAR BIOLOGY-
自引率
9.10%
发文量
13
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信