食品科学

• 生物工程 • 上一篇    下一篇

长双歧杆菌α-半乳糖苷酶的分离纯化及酶学性质

陈俊亮,田 芬,霍贵成,张慧芸   

  1. 1.河南科技大学食品与生物工程学院,河南 洛阳 471003;2.东北农业大学 乳品科学教育部重点实验室,
    黑龙江 哈尔滨 150030;3.杭州娃哈哈集团有限公司研究院,浙江 杭州 310018
  • 出版日期:2014-04-15 发布日期:2014-04-18

Purification and Characterization of α-Galactosidase from Bifidibacterium longum

CHEN Jun-liang, TIAN Fen, HUO Gui-cheng, ZHANG Hui-yun   

  1. 1. College of Food and Bioengineering, Henan University of Science and Technology, Luoyang 471003, China;
    2. Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin 150030, China;
    3. Research Institute of Hangzhou Wahaha Group Company Limited, Hangzhou 310018, China
  • Online:2014-04-15 Published:2014-04-18

摘要:

对长双歧杆菌KLDS2.0509所分泌的α-半乳糖苷酶进行分离纯化,并对其酶学性质进行研究。经过聚丙烯酰胺凝胶电泳,此酶的分子质量约为45 kD;酶学性质研究表明,该酶最适作用pH值为5.0,最适温度42 ℃;大多数金属离子对酶的活性无显著影响,Fe2+、Mn2+、Ag+和Cu2+能够对其产生抑制作用,而Hg2+完全抑制酶活性;该酶可降解蜜二糖、棉子糖和水苏糖,但不能降解末端含α-半乳糖苷键的多糖。

关键词: 长双歧杆菌, &alpha, -半乳糖苷酶, 分离纯化, 酶学性质

Abstract:

An α-galactosidase from Bifidibacterium longum KLDS2.0509 was purified by ammonium sulfate precipitationand Sephadex G-100 filtration chromatography, and its enzymatic properties were characterized. The molecular weightof the purified enzyme was approximately 45 kD as determined by SDS-PAGE. The optimal pH and temperature of theenzyme were pH 5.0 and 42 ℃, respectively. The α-galactosidase activity was not significantly influenced by most of theinvestigated metal ions, but slightly inhibited by Fe2+, Mn2+, Ag+ and Cu2+, and completely inhibited by Hg2+. This enzymewas able to degrade natural substrates such as melibiose, raffinose and stachyose, but could not degrade galactose-containingpolysaccharides.

Key words: Bifidibacterium longum, α-galactosidase, purification, enzymatic properties