›› 2012, Vol. 14 ›› Issue (2): 73-80.DOI: 10.3969/j.issn.1008-0864.2012.02.12

• 生物技术 生命科学 • 上一篇    下一篇

细菌Ⅰ型普鲁兰酶的研究进展

孙晓晨,初晓宇,伍宁丰   

  1. (中国农业科学院生物技术研究所, 北京 100081)
  • 收稿日期:2011-09-13 修回日期:2011-12-05 出版日期:2012-04-15 发布日期:2012-04-13
  • 通讯作者: 伍宁丰,研究员,主要从事微生物分子生物学与基因工程研究。Tel:010-82109844; E-mail:wunf@caas.net.cn
  • 作者简介:孙晓晨,硕士研究生,研究方向为微生物分子生物学与基因工程。Tel:010-82109864|E-mail:xchsun09@yahoo.cn。
  • 基金资助:

    中国农业科学院生物技术研究所基本科研业务费专项基金(1610392011008)资助。

Research Progress in Type Ⅰ Pullulanase from Bacteria

SUN Xiao-chen, CHU Xiao-yu, WU Ning-feng   

  1. (Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China)
  • Received:2011-09-13 Revised:2011-12-05 Online:2012-04-15 Published:2012-04-13

摘要:

Ⅰ型普鲁兰酶以内切的方式专一性作用于普鲁兰糖或者支链多糖的α-1,6糖苷键,生成产物麦芽三糖或线性多糖。在工业应用中,Ⅰ型普鲁兰酶与其他糖苷水解酶协同作用于不同糖类底物,可得到类型多样的终产物,因此在食品、化工、制药等行业中有很重要的作用。目前对Ⅰ型普鲁兰酶的研究不仅包括筛选高产酶的菌株,还需得到酶学性质优良的酶蛋白,以适合工业生产工艺。综述了细菌来源的Ⅰ型普鲁兰酶的研究概况,包括酶学性质、基因的分离与克隆、微生物生产,并讨论了该酶在工业生产中的应用及其研究前景。

关键词: Ⅰ型普鲁兰酶;细菌;支链多糖

Abstract:

TypeⅠpullulanase typically hydrolyzes the α-1,6 glucosidic linkages of pullulan or branched oligosaccharides in an endo-way to produce maltotriose or liner oligosaccharides, respectively. This enzyme plays a very significant role in the food, chemistry and medical industries, because they can degrade different saccharides with other glycoside hydrolases producing various products. At present, studies on this enzyme focus not only on screening novel strains, but also on obtaining type Ⅰ pullulanase with proper properties to suit industrial production. This review summarizes the research progress on type Ⅰ pullulanase from bacteria in some fields, such as catalytic properties, separation and cloning of gene, producing enzyme by microorganism. The industrial application of this enzyme and prospect of its research are also discussed.

Key words: type Ⅰ pullulanase, bacteria, amylopectin

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