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[1]李彧娜,石贵阳,王武,等.Rhizopus microsporus var. chinensis生淀粉糖化酶的分离纯化及酶学性质[J].应用与环境生物学报,2010,16(05):714-718.[doi:10.3724/SP.J.1145.2010.00714]
 LI Yuna,SHI Guiyang,WANG Wu,et al.Purification and Properties of a Novel Raw Starch Digesting Glucoamylase from Rhizopus microsporus var. chinensis[J].Chinese Journal of Applied & Environmental Biology,2010,16(05):714-718.[doi:10.3724/SP.J.1145.2010.00714]
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Rhizopus microsporus var. chinensis生淀粉糖化酶的分离纯化及酶学性质()
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《应用与环境生物学报》[ISSN:1006-687X/CN:51-1482/Q]

卷:
16卷
期数:
2010年05期
页码:
714-718
栏目:
研究论文
出版日期:
2010-10-25

文章信息/Info

Title:
Purification and Properties of a Novel Raw Starch Digesting Glucoamylase from Rhizopus microsporus var. chinensis
文章编号:
200912006
作者:
李彧娜石贵阳王武王正祥
(江南大学生物工程学院生物资源与生物能源研究中心和工业生物技术教育部重点实验室 无锡 214122)
Author(s):
LI YunaSHI GuiyangWANG WuWANG Zhengxiang
(Research Center of Bioresource and Bioenergy, School of Biotechnology, Jiangnan University and Key Laboratory of Industrial Biotechnology, Ministry of Education, Wuxi 214122, Jiangsu, China)
关键词:
生淀粉糖化酶Rhizopus microsporus var. chinensis纯化酶学性质
Keywords:
raw starch digesting glucoamylase Rhizopus microsporus var. chinensis purification enzymatic property
分类号:
Q936 : TQ925
DOI:
10.3724/SP.J.1145.2010.00714
文献标志码:
A
摘要:
从Rhizopus microsporus var. chinensis CICIM F0088菌株中分离纯化一种新的具有生淀粉降解能力的糖化酶,并研究其酶学性质. 经硫酸铵沉淀、双水相交换、DEAE-650M 阴离子层析、Bio-Rad 制备电泳等步骤后获得电泳均一的糖化酶,其相对分子质量约为52×103. 该酶最适反应pH为4.5,在pH 3.5~6.5范围内稳定;最适反应温度为75 ℃,具有较宽的pH耐受范围和较高的温度耐受性. 经飞行质谱分析得到酶蛋白中3个肽段的氨基酸序列,通过比对发现,该酶与NCBI中已报道的糖化酶序列具有一定的同源性. 图6 表1 参18
Abstract:
A novel raw starch digesting glucoamylase from Rhizopus microsporus var. chinensis was purified by sequential ammonium sulfate precipitation, aqueous two-phase systems (ATPS), DEAE-650M chromatography and Bio-Rad Prep Cell. The protein performed a ralative molecular mass of 52×103 estimated by SDS-PAGE. The purified glucoamylase behaved the maximum activity at pH 4.5 and was stable between pH 3.5 to 6.5. Furthermore, the enzyme exhibited the maximum activity at 75 ℃. The amino acid sequences of three peptides from the purified enzyme were analyzed by LTQ (Liquid chromatography-ion trap mass spectrometry), and those peptides compared with that of reported glucoamylase amino acid sequence in NCBI was similar in some extent. Fig 6, Tab 1, Ref 18

参考文献/References:

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备注/Memo

备注/Memo:
国家高技术研究发展计划“863”项目(No. 2006AA020204)资助 Supported by the National High-tech R & D Program of China (No. 2006AA020204)
更新日期/Last Update: 2010-10-25