Heterologous expression of a GH3 beta-glucosidase from Neurospora crassa in Pichia pastoris with high purity and its application in the hydrolysis of soybean isoflavone glycosides
文献类型：期刊论文
| 作者 | Pei, Xue1,2; Zhao, Junqi2; Cai, Pengli2; Sun, Wenliang2; Ren, Jie2; Wu, Qiaqing2; Zhang, Shihong1; Tian, Chaoguang2 |
| 刊名 | PROTEIN EXPRESSION AND PURIFICATION
 |
| 出版日期 | 2016-03-01 |
| 卷号 | 119页码:75-84 |
| 关键词 | Neurospora crassa beta-glucosidase Isoflavone glycosides Pichia pastoris |
| 英文摘要 | Previous studies have shown isoflavone aglycones to have more biological effects than their counterparts, isoflavone glycones. Some beta-glucosidases can hydrolyze isoflavone glucosides to release aglycones, and discovery of these has attracted great interest. A glycoside hydrolase (GH) family 3 beta-glucosidase (bgl2) gene from Neurospora crassa was heterologously expressed in Pichia pastoris with high purity. The recombinant BGL2 enzyme displayed its highest activity at pH 5.0 and 60 degrees C, and had its maximum activity against p-nitrophenyl-beta-D-glucopyranoside (pNPG) (143.27 +/- 4.79 U/mg), followed by cellobiose (74.99 +/- 0.78 U/mg), gentiobiose (47.55 +/- 0.15 U/mg), p-nitrophenyl-beta-D-cellobioside (pNPC) (40.07 +/- 0.87 U/mg), cellotriose (1231 +/- 0.36 U/mg) and cellotetraose (9.04 +/- 0.14 U/mg). The kinetic parameters of K-m and Vmax were 0.21 +/- 0.01 mM and 147.93 +/- 2.77 mu M/mg/min for pNPG. The purified enzyme showed a heightened ability to convert the major soybean isoflavone glycosides (daidzin, genistin and glycitin) into their corresponding aglycone forms (daidzien, genistein and glycitein). With this activity against soybean isoflavone glycosides, BGL2 shows great potential for applications in the food, animal feed, and pharmaceutical industries. (C) 2015 Elsevier Inc. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 关键词[WOS] | BACILLUS-SUBTILIS NATTO ; BIOCHEMICAL-CHARACTERIZATION ; PAECILOMYCES-THERMOPHILA ; THERMOASCUS-AURANTIACUS ; FUNCTIONAL EXPRESSION ; CRYSTAL-STRUCTURES ; DEGRADING ENZYMES ; CLONING ; HYDROLASE ; PURIFICATION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000368966800011 |
| 源URL | [http://124.16.173.210/handle/834782/1541]  |
| 专题 | 天津工业生物技术研究所_微生物功能基因组学与生物技术实验室 田朝光_期刊论文 |
| 作者单位 | 1.Jilin Univ, Coll Plant Sci, Changchun 130062, Peoples R China 2.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin 300308, Peoples R China |
| 推荐引用方式 GB/T 7714 | Pei, Xue,Zhao, Junqi,Cai, Pengli,et al. Heterologous expression of a GH3 beta-glucosidase from Neurospora crassa in Pichia pastoris with high purity and its application in the hydrolysis of soybean isoflavone glycosides[J]. PROTEIN EXPRESSION AND PURIFICATION,2016,119:75-84. |
| APA | Pei, Xue.,Zhao, Junqi.,Cai, Pengli.,Sun, Wenliang.,Ren, Jie.,...&Tian, Chaoguang.(2016).Heterologous expression of a GH3 beta-glucosidase from Neurospora crassa in Pichia pastoris with high purity and its application in the hydrolysis of soybean isoflavone glycosides.PROTEIN EXPRESSION AND PURIFICATION,119,75-84. |
| MLA | Pei, Xue,et al."Heterologous expression of a GH3 beta-glucosidase from Neurospora crassa in Pichia pastoris with high purity and its application in the hydrolysis of soybean isoflavone glycosides".PROTEIN EXPRESSION AND PURIFICATION 119(2016):75-84. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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