搜索页_ α-Amylase

设为首页

收藏本站

网站地图 | English | 公务邮箱

读者指南

学术客户端

NSTL服务站

科技查新

外文资源

Springer电子图书(2)	NATURE电子期刊(10)	Elsevier电子期刊(204)
SpringerLink电子期刊(660)	GSW全文库(1)	ACS电子期刊(20)

在“Elsevier电子期刊”中，命中：204条，耗时：小于0.01 秒

在所有数据库中总计命中：897条

1.Interactions between α-amylase and an acidic branched polysaccharide from green tea

作者：Shuyun Wu ; Minghua Lai ; Jiahao Luo ; Jingwen Pan ; Li-Ming Zhang ; Liqun Yang ; ^{yanglq@mail.sysu.edu.cn}

关键词：Branched acidic tea polysaccharide ; α-amylase ; Interaction

刊名：International Journal of Biological Macromolecules

出版年：2017

2.Molecular dynamics and protein interaction studies of lipopeptide (Iturin A) on α- amylase of Spodoptera litura

作者：P. Narendra Kumar^a ; T.H. Swapna^a ; Mohamed Yahya Khan^a ; Jayasimha Rayalu Daddam^b ; Bee Hameeda^a ; ^{drhami2009@gmail.com}

关键词：Molecular Dynamics ; Docking studies ; α- amylase ; Modeller7v7 ; Iturin A ; Insecticidal activity

刊名：Journal of Theoretical Biology

出版年：2017

3.Microbial α-amylase: A biomolecular overview

作者：Qiaoge Zhang ^{qiaogezhang@tju.edu.cn} ; Ye Han ; ^{hanye@tju.edu.cn} ; Huazhi Xiao

关键词：Microbial α-amylase ; Biomolecular basis ; Gene ; Structure ; Database

刊名：Process Biochemistry

出版年：2017

4.New polyhydroxytriterpenoid derivatives from fruits of Terminalia chebula Retz. and their α-glucosidase and α-amylase inhibitory activity

作者：Dong Young Lee^a ; Heejung Yang^b ; Hyun Woo Kim^a ; Sang Hyun Sung^a ; ^{shsung@snu.ac.kr}

关键词：Polyhydroxytriterpenoids ; Terminalia chebula ; α-Glucosidase ; α-Amylase

刊名：Bioorganic & Medicinal Chemistry Letters

出版年：2017

5.Comparison of α-amylase, α-glucosidase and lipase inhibitory activity of the phenolic substances in two black legumes of different genera

作者：Yuqing Tan ^{yt142@msstate.edu" class="auth_mail" title="E-mail the corresponding author} ; Sam K.C. Chang ; ^{sc1690@msstate.edu" class="auth_mail" title="E-mail the corresponding author} ; Yan Zhang ^{yzhang@fsnhp.msstate.edu" class="auth_mail" title="E-mail the corresponding author}

关键词：Phenolic compounds ; Lipase ; α-Glucosidase and α-amylase inhibition

刊名：Food Chemistry

出版年：2017

6.Number of branch points in α-limit dextrins impact glucose generation rates by mammalian mucosal α-glucosidases

作者：Byung-Hoo Lee^a ; Bruce R. Hamaker^b ; ^{hamakerb@purdue.edu}

关键词：α-limit dextrins ; Starch ; Slow digestion ; α-glucosidases ; Human α-amylase

刊名：Carbohydrate Polymers

出版年：2017

7.Rb2 inhibits α-glucosidase and regulates glucose metabolism by activating AMPK pathways in HepG2 cells

作者：Hui Teng¹ ; Lei Chen¹ ; ^{chenlei841114@hotmail.com} ; Ting Fang ; ^{fangting930@163.com} ; Benyao Yuan ; Qiyang Lin

关键词：Rb2 ; α-Glucosidase ; α-Amylase ; Glucose metabolism ; AMPK

刊名：Journal of Functional Foods

出版年：2017

8.Development of a workflow for screening and identification of α-amylase inhibitory peptides from food source using an integrated Bioinformatics-phage display approach: Case study - Cumin seed

作者：Hwee-Leng Siow^a ; Theam Soon Lim^b ; ^{theamsoon@usm.my" class="auth_mail" title="E-mail the corresponding author} ; Chee-Yuen Gan^a ; ^{cygan@usm.my" class="auth_mail" title="E-mail the corresponding author}

关键词：α-Amylase inhibition ; Bioactive peptide discovery ; Bioinformatics ; Phage display

刊名：Food Chemistry

出版年：2017

9.Effect of the glass transition temperature on alpha-amylase activity in a starch matrix

作者：Vinita Chaudhary ; Naksit Panyoyai ; Darryl M. Small ; Robert A. Shanks ; Stefan Kasapis ; ^{stefan.kasapis@rmit.edu.au}

关键词：Starch ; Maltodextrin ; α-Amylase ; Glass transition temperature ; Activation energy

刊名：Carbohydrate Polymers

出版年：2017

10.Halloysite nanotubes - An efficient ‘nano-support’ for the immobilization of α-amylase

作者：Gaurav Pandey ; Diogos Marcos Munguambe ; Maithri Tharmavaram ; Deepak Rawtani ; ^{rawtanid@gmail.com} ; Y.K. Agrawal

关键词：Halloysite nanotubes ; Amylase ; Immobilized enzyme ; Clay ; Enzyme activity

刊名：Applied Clay Science

出版年：2017

按检索点细分(204)

题名(82)

关键词(92)

文摘(151)

按出版年细分(204)

2017年(32)

2016年(144)

2015年(26)

2011年(2)

常见问题　|　交通位置　|　联系我们　|　OA远程办公

地址：北京市海淀区学院路29号邮编：100083

电话：办公室：(+86 10)66554848；文献借阅、咨询服务、科技查新：66554700