基本介绍

内容简介

《环糊精——科学与技术》由国内食品科学领域知名专家金征宇教授倾心打造，就超分子科学中的重要分支——环糊精做了全面详细的介绍，体现了具有国际领先水平的最新科研成果。不仅详细介绍了环糊精科学的进展，同时还对环糊精的工业和非工业应用做了详细介绍，尤其是在活性食品包装中的应用。 《环糊精——科学与技术》受到了国际知名学者及国外出版公司的一致好评。

作者简介

金征宇，江南大学，副校长，教授，本选题主要涉及碳水化合物资源开发与利用领域： 先后在英国糖业技术研究中心、荷兰WAGENINGEN大学、美国KANSAS STATE UNIVERSITY 等从事博士后以及访问教授研究工作。 现任江南大学食品科学与技术国家重点实验室主任、食品科学与工程国家一级重点学科带头人，兼任国务院学位委员会食品学科评议组召集人、科技部“十二五”食品科技战略研究总体专家组组长、中国粮油学会副理事长。 在功能性碳水化合物资源开发与利用领域成果显著，得到国家科技支撑重大项目、国家自然科学基金重点项目和国家“863”计划资助，获国家科技进步二等奖3项（2007，2009，2011）、国家教学成果二等奖2项（2001，2005），所指导的博士生2010年获全国百篇优秀博士学位论文奖。

图书目录

Preface Acknowledgment 1.Introduction Jun-Rong Huang, Hai-Ning Zhuang and Zheng-Yu Jin 1.2 Nomenclature,Classification,Structure and Property 1.2.1 Nomenclature 1.2.2 Classification 1.2.3 Struvture 1.2.4 Property 1.3 Inclusion Complex Formation,Preparation 1.3.1 Formation of inclusion complexes 1.3.2 Methods ofpreparation of inclusion complexes 1.3.3 Characterization of inclusion complexes 2.Enzymes in Preparing Cyclodextrins Shengjun Wu, Xiu-Ting Hu,Jin-Moon kim and Jing Chen 2.1Introduction 2.2CGTase 2.2.1 The catalytic mechanism of CGTase 2.2.1.1 The structure of CGTase 2.2.1.1.1 The primary structure of CGTase 2.2.1.1.2 The domain and active centers of CGTase 2.2.1.2 The catalytic mechanism of CGTase 2.2.1.3 The advancesin the product specificity of CGTase research 2.2.2 Classification of CGTase and their bacteria sources 2.2.2.1 Classification of CGTase 2.2.2.2 Bacteria source of CGTase 2.2.3 The enzymatic properties of CGTase 2.2.3.1 The nature ofCGTase from Baallus 2.2.3.1.1 Molecularweight 2.2.3.1.2 Kineticconstants(Kmand Vmax) 2.2.3.1.30ptimum pH and pH stability 2.2.3.1.4 Optimum temperature and thermalstability 2.2.3.1.5 Effect of metalions on theenzyme activity 2.2.3.2 The nature of CGTase from B.alkalophilus sp.G1 2.2.3.2.1 Molecular weight 2.2.3.2.2 Kinetic constants (Km and V max) 2.2.3.2.3 Optimum pH and pH stability 2.2.3.2.4 Optimum temperature and temperature stability 2.2.3.2.5 Effect of metalions and other reagents on the activity of CGDTase 2.3 Preparation of CGTase by Fermentation 2.3.1 The types and the expansion of cultivation of the bacteria for preparation of CGTase 2.3.2 Controloffermentation conditions of CGTase 2.3.2.1 Medium composition 2.3.2.1.2 Nitrogen source 2.3.2.5 Immobilized production of CGTase 2.3.3 Determination of CGTase activity 2.4 Purification ofCGTase 2.4.1 Pretreatment and filtration offermentation broth 2.4.1.2 Organic solvent precipitation 2.4.2 Concentration and precipitation of crude enzyme solution 2.4.3.1 Affinity chromatography 2.4.3.2 Ion-exchange chromatography 2.4.3.3 Gel filtration or gelpermeation chromatography 2.4.3.4 Dialysis 2.5 The Substrate Catalysis Characteristics and Sources of Pullulanase 2.5.1 The substrate catalysis characteristics pullulanase 2.5.2 Source of pullulanase 2.6 The Substrate Catalysis Characteristics and Sources of Isoamylase 2.6.1 The substrate catalysis characteristics and of isoamylase 2.6.2 The source of isoamylase 2.7 The Source and Nature of Galactosidase 2.7.1 α-Galactosidase 2.7.1.1 The source of α-galactosidase 2.7.1.2 The transferase activity of α-galactosidase 2.7.2 β-galactosidase 2.7.2.1 Source of β-galactosidase 2.7.2.2 The transferase activity of β-galactosidase 2.8 Immobilization of the Enzymes for CD Preparation 2.8.1 Preparation of immobilized enzyme 2.8.1.1.1 Physicaladsorption 2.8.1.1.2 Ion exchange adsorption 2.8.1.1.3 The methods ofpreparation of the immobilized enzyme adsorption 2.8.1.2 Covalentbinding method 2.8.1.2 Covalent bingding method 2.8.1.3 Crosslinking 2.8.1.4 Embedding 2.8.2 Properties and application of immobilized enzyme 2.8.2.1 Immobilized enzyme activity 2.8.2.2 The catalytic properties of immobilized enzyme 2.8.2.2.1 Substrate specifiaty 2.8.2.2.2 The optimum pH of enzyme 2.8.2.2.3 The optimum temperature or theimmobilized enzyme 2.8.2.2.4 Michaelis constant (Km) and maximum reaction rate 2.8.2.3 Immobilized enzyme stability 2.8.2.3.1 Thermal stability 2.8.2.3.2 The stability toward various reagents 2.8.2.3.3 Stability toward protease 2.8.2.3.4 Operational stability 2.8.2.3.5 Storage stability References 3.Preparation andAnalysis ofCyclodextrin An- Wei Cheng and Jin-Peng Wang and Zheng- Yu Jin 3.1 Introduction 3.1.1 Enzymatic preparation of cyclodextrins 3.1.1.1 Non-controlsystem (add non-organicsolvent) 3.1.1.2 Controlsystem(addorganicsolvent) 3.1.2 Influence factors for CDs preparation 3.1.2.2 Reaction substrate 3.1.2.4 Temperature 3.1.2.6 Organic solvent addition 3.2 Industrial Process for α-Cyclodextrin Preparation 3.2.1 Control system 3.2.2 Non-control system 3.3 IndustrialProcess for β-Cyclodextrin Preparation 3.3.1 Control system 3.3.2 Non-controlsystem 3.4 The Preparation of γ-Cyclodextrin 3.4.1 Controlsystem 3.4.2 Non-controlsystem 3.5 Preparation of theLR-CDs 3.5.1 Enzyme for LR-CDs preparation 3.5.2 Process of LR-CDspreparation 3.5.3 Separation and purification of LR-CDs 3.6 Quantitative and Qualitative Analysis for Cyclodextrin 3.6.1 Cyclodextrin quantitative analysis 3.6.1.1 UV spectrophotometry 3.6.1.2 High performanceliquid chromatography 3.6.2 Cyclodextrin qualitative analysis 3.6.2.1 Paper chromatography and thin layer chromatography 3.6.2.2 Gas chromatography 3.6.2.3 Capillaryelectrophoresis 3.6.2.4 High performance anion-exchange chromatography with pulsed amperometric detection 3.6.2.5 Mass spectrometry and nuclear magnetic resonance References 4.Preparation ofBranched- Cyclodextrins Xing Zhou, Yao-Qi Tian and Zheng- Yu Jin 4.1 BasicTheories 4.1.1 Synthesis mechanisms 4.1.2 Using CD and maltodextrin/starch as raw material 4,1.3 Using CD and a-maltosyl fluoride (α-G2F) asrawmaterial 4.1.4 The preparation of galactosidase and enzymatic preparation of Gal-CD 4.2 Preparation of Mal-CDs 4.2.1 Reaction conditions 4.2.1.1 Pullulanase activity 4.2.1.2 Optimization of the production of Mal-β-CD by pullulanase 4.2.1.2.1 pH value 4.2.1.2.2 Temperature …… 5.Preparation and Analysis of Cyclodextrin Derivatives Chao Yuan, Yu-Xiang Bai and Zheng- Yu Jin 7.Use of Cyclodextrins in Food, Pharmaceutical and Cosmetic Industries Yao-Qi Tian, Xing Zhon and Zheng- Yu Jin