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研究生： 王福玲
Nathania Puspitasari
論文名稱： 重組疏水蛋白增強酶水解聚對苯二甲酸乙二酯(PET) 及 PETase 應用於 PET 材料之表面功能化應用
Enhanced Enzymatic Hydrolysis of Poly(ethylene terephthalate) (PET) by Recombinant Hydrophobins and PET Surface Functionalization via PETase Hydrolysis
指導教授： 李振綱
Cheng-Kang Lee
口試委員: 李振綱
王勝仕
蔡伸隆
鄭光成
Kuan-Chen Cheng
學位類別： 博士
Doctor
系所名稱： 工程學院 - 化學工程系
Department of Chemical Engineering
論文出版年： 2021
畢業學年度： 109
語文別： 英文
論文頁數： 173
中文關鍵詞： 疏水蛋白 、PETase 、角質酶 、重组蛋白 、PET 回收 、纤维素结合域 、lysostaphin 、细菌纤维素 、一氧化氮 、抗菌
外文關鍵詞： Hydrophobin, PETase, cutinase, recombinant protein, PET recycling, cellulose binding domain, lysostaphin, bacterial cellulose, nitric oxide, antibacterial
相關次數： 點閱：219  下載：0 
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    • COVER i DOCTORAL DISSERTATION ADVISOR RECOMENDATION ii QUALIFICATION FORM BY DOCTORAL DEGREE EXAMINATION COMMITTEE iii CHINESE ABSTRACT iv ENGLISH ABSTRACT vi ACKNOWLEDGEMENT viii TABLE OF CONTENTS ix LIST OF ABBREVIATIONS xiv LIST OF TABLES xvi LIST OF FIGURES xvii CHAPTER 1 INTRODUCTION 1 1.1. General introduction 2 1.2. Objectives 3 1.3. References 4 CHAPTER 2 LITERATURE REVIEW 7 2.1. Poly(ethylene terephthalate) (PET) 8 2.1.1 Properties and application 8 2.1.2 Synthesis process 8 2.1.3 PET disposal and recycling methods 9 2.2. Enzymatic hydrolysis of PET 10 2.2.1. Cutinase 13 2.2.2 Poly(ethylene terephthalate) hydrolase (PETase) 14 2.2.3. Potential chassis for PET hydrolases production 14 2.2.4. Challenges in enzymatic PET hydrolysis 15 2.2.5. Methods for improving the catalytic activity of PET hydrolases 15 2.3. Hydrophobins 17 2.4. Cellulose binding domain (CBD) 19 2.5. Bacterial cellulose (BC) 20 2.6. Lysostaphin 21 2.7. Nitric oxide (NO) 22 2.7.1. Antibacterial mechanism of NO 23 2.7.2. Methods for NO release detection 24 2.7.3. NONOate conjugated NO-releasing polymeric materials 24 2.8. References 26 CHAPTER 3 CLASS I HYDROPHOBINS PRETREATMENT ENHANCED ENZYMATIC HYDROLYSIS FOR MONOMERS RECYCLING OF WASTE PET 33 3.1. Introduction 34 3.2. Experimental section 36 3.2.1. Materials and chemicals 37 3.2.2. Plasmid, strains, and media 37 3.2.3. Cloning, expression, and purification of recombinant Cutinase 38 3.2.3.1. Production of Cutinase from wild-type Thermobifida fusca 38 3.2.3.2. Construction of recombinant plasmids 38 3.2.3.3. Preparation of E. coli competent cell 39 3.2.3.4. Transformation of competent E. coli 39 3.2.3.5. Colony PCR for the selection of positive clones 39 3.2.3.6. Agarose gel electrophoresis 40 3.2.3.7. Expression and purification of recombinant cutinases 40 3.2.3.8. SDS-PAGE analysis 41 3.2.4. Expression and purification of recombinant PETase 42 3.2.5. Activity assay of esterase enzyme 42 3.2.6. Production of class I hydrophobins 43 3.2.6.1. Isolation of native hydrophobin RolA 43 3.2.6.2. Expression and purification of recombinant hydrophobins 43 3.2.6.3. Characterization of class I hydrophobins 44 3.2.7. Enzymatic hydrolysis of PETs 44 3.2.8. HPLC analysis 45 3.2.9. SEM analysis 45 3.3. Results and discussions 45 3.3.1. Cloning, expression, and purification of recombinant cutinases 45 3.3.2. Expression and purification of recombinant PETase 48 3.3.3. Enzymatic PET hydrolysis by esterase enzymes 50 3.3.3.1. PETase hydrolysis 50 3.3.3.2. Cutinase hydrolysis 56 3.3.4. Production of class I hydrophobins 58 3.3.4.1. Native hydrophobin RolA 58 3.3.4.2. Recombinant hydrophobins 58 3.3.4.3. Characterization of the proteins 60 3.3.5. Effect of hydrophobins on PETase hydrolysis 62 3.4. References 67 CHAPTER 4 SOLUBLE EXPRESSION OF CLASS I HYDROPHOBIN BY FUSION WITH CELLULOSE BINDING DOMAIN AND ITS PURIFICATION USING BACTERIAL CELLULOSE 71 4.1. Introduction 72 4.2. Experimental section 73 4.2.1. Plasmids, strains, and media 74 4.2.2. Construction of recombinant CBD-HGFI 74 4.2.3. Expression and purification of fusion protein using IMAC 75 4.2.4. Production of bacterial cellulose 75 4.2.5. One-step purification and immobilization of CBD fusion on BC 76 4.2.6. Characterization of purified CBD fused HGFI 77 4.2.7. Enzymatic hydrolysis of PET 78 4.3. Results and discussions 79 4.3.1. Cloning, expression, and purification of recombinant CBD-HGFI 79 4.3.2. Simultaneous purification and immobilization of CBD fusion on BC 81 4.3.3. Properties analysis of purified CBD fused HGFI 86 4.3.4. Effect of hydrophobins pretreatment on PETase hydrolysis 91 4.4. References 92 CHAPTER 5 IMPROVED PET-HYDROLYZING ENZYMES ACTIVITY BY GENETIC FUSION TO CLASS I HYDROPHOBIN 96 5.1. Introduction 97 5.2. Experimental section 98 5.2.1. Materials and chemicals 98 5.2.2. Plasmids and strains 98 5.2.3. Construction of fusion proteins 99 5.2.4. Expression and purification of fusion proteins 100 5.2.5. Activity assay of esterase enzyme 100 5.2.6. Characterization of hydrophobin fusion proteins 100 5.2.7. Enzymatic hydrolysis of PET fiber 101 5.3. Results and discussions 101 5.3.1. Cloning, expression, and purification of recombinant CBD-HGFI-PETase 101 5.3.2. Cloning, expression, and purification of recombinant HGFI-Cut_2 103 5.3.3. Characterization of fusion proteins 106 5.3.4. Effect of hydrophobins fused enzymes on PET fiber hydrolysis 107 5.4. References 109 CHAPTER 6 SURFACE FUNCTIONALIZATION OF PETASE-TREATED PET FIBER WITH NITRIC OXIDE RELEASING FOR ANTIBACTERIAL AGENT 111 6.1. Introduction 112 6.2. Experimental section 114 6.2.1. Materials 114 6.2.2. Bacteria and enzyme 114 6.2.3. Preparation of PEI-grafted PET fiber 114 6.2.4. Preparation of NO-conjugated PET fiber 115 6.2.5. Characterization 115 6.2.6. Antibacterial test 116 6.3. Results and discussions 117 6.3.1. Preparation and characterization of PEI-grafted carboxylated PET fiber 117 6.3.2. NO conjugation to PEI-grafted PET fiber 121 6.3.3. Antibacterial activity of NO-conjugated PET fiber 123 6.4. References 125 CHAPTER 7 CONCLUSIONS AND FUTURE PERSPECTIVES 129 7.1. Conclusions 130 7.2. Future perspectives 131 APPENDIX 133 AUTOBIOGRAPHY 150

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