系統識別號 | U0002-1306201709535100 |
---|---|
DOI | 10.6846/TKU.2017.00406 |
論文名稱(中文) | Euonymus laxiflorus Champ 以及 Paenibacillus sp. TKU042 所生產α-葡萄糖苷酶抑制劑與α-澱粉酶抑制劑之研究 |
論文名稱(英文) | The studies on α‐glucosidase and α‐amylase inhibitors from Euonymus laxiflorus Champ and Paenibacillus sp. TKU042 |
第三語言論文名稱 | |
校院名稱 | 淡江大學 |
系所名稱(中文) | 化學學系博士班 |
系所名稱(英文) | Department of Chemistry |
外國學位學校名稱 | |
外國學位學院名稱 | |
外國學位研究所名稱 | |
學年度 | 105 |
學期 | 2 |
出版年 | 106 |
研究生(中文) | 阮文邦 |
研究生(英文) | Van-Bon Nguyen |
學號 | 803160117 |
學位類別 | 博士 |
語言別 | 英文 |
第二語言別 | |
口試日期 | 2017-05-22 |
論文頁數 | 84頁 |
口試委員 |
指導教授
-
王三郎(sabulo@mail.tku.edu.tw)
委員 - 謝淳仁(cjshieh@nchu.edu.tw) 委員 - 王三郎(sabulo@mail.tku.edu.tw) 委員 - 王全祿(chuanlu@mail.fit.edu.tw) 委員 - 糜福龍(flmi530326@tmu.edu.tw) 委員 - 郭耀豪(kuoyh@nricm.edu.tw) |
關鍵字(中) |
抑制劑 大丁黃 糖尿病 類芽孢桿菌 微生物轉換 |
關鍵字(英) |
Inhibitors Euonymus laxiflorus Champ diabetes Paenibacillus microbial conversion |
第三語言關鍵字 | |
學科別分類 | |
中文摘要 |
本研究將收集自越南得樂省之二十六種中草藥進行α-葡萄糖 苷酶及α-澱粉酶抑制活性之分析。結果顯示大丁黃之甲醇萃取物 具有最高抑制活性。自此大丁黃萃取物分離出十一種具抑制活性之 化合物。其中三種(1,10,11)為新化合物,兩種為已知結構但新 發現具有α-澱粉酶抑制活性之化合物(13,21),以及已知之酚類 化合物(2,9,16,17,18,19)。其中六種化合物(1,2,9, 13,16,17)具有與阿卡波糖這種糖尿病用藥不相上下之抑制活 性。此外自台灣土壤所篩選超過六百株細菌當中,類芽孢桿菌 TKU042 具有最佳α - 葡萄糖苷酶抑制活性。此菌發酵營養液 (nutrient broth)所得抑制活性高於阿卡波糖且具耐熱及酸鹼安 定性,小鼠降血糖試驗結果亦經證實。這些結果顯示,大丁黃及類 芽孢桿菌TKU042 發酵液具有應用於控制糖尿病及減肥之類保健食 品之潛力。 |
英文摘要 |
The present study was aimed at finding safe, natural and abundant source of α-glucosidase and α-amylase inhibitors (αGIs and αAIs). Twenty-six samples of medicinal plants were collected in the Dak Lak province of Vietnam and evaluated for αGIs and αAIs. Trunk bark extract from Euonymus laxiflorus Champ (ELC) was selected as the best source of these inhibitors. Eleven novel active compounds were successfully isolated from ELC. Five compounds (1, 10, 11, 13 and 21) were determined as new aAIs in which 3 inhibitors (1, 10 and 11) were identified as new compounds. Another 6 compounds (2, 9, 16, 17, 18, and 19) were confirmed as known phenolic compounds. Notably, 6 compounds (1, 2, 9, 13, 16 and 17) showed a potency of slightly higher or comparable inhibition to that of acarbose. Among more than 600 bacterial strains isolated from Taiwanese soils, Paenibacillus sp. TKU042 was selected as the best producer of aGIs. The supernatant of fermented nutrient broth (FNB) showed stronger inhibitory activities than acarbose. The FNB aGIs also showed high thermal and pH stability, and acceptable effect on reducing plasma glucose in mice. All of the results suggest that ELC and FNB could have potential use for type 2 diabetes and obesity treatments or health foods development. |
第三語言摘要 | |
論文目次 |
Introduction 1 Diabetes mellitus (DM) 1 Indigenous medicinal plants in Central Higland of Vietnam, potential sources of natural bio-active compounds 1 Microbial fermentation, a potent and effective tool for production of natural bioactive materials 3 Chapter 1. Screening and evaluation of α-glucosidase inhibitors from indigenous medicinal plants in Dak Lak Province, Vietnam 8 1.1.Introduction 8 1.2. Results and Discussion 9 1.2.1. Screening and evaluation of α-glucosidase inhibition 9 1.2.2. Inhibitory activity of the ELC extract against α-glucosidase from S. cerevisiae 10 1.2.3. The pH and thermal stabilities of the ELC extract 12 1.2.4. Inhibitory activity of the ELC extract against some enzymes 13 1.2.5. The influence of reaction time on the inhibitory activity of the extract against some enzymes 15 1.3. Experimental Section 15 1.3.1. Materials 15 1.3.2. Extraction method 16 1.3.3. Rat intestinal α-glucosidase inhibition screening assay 16 1.3.4. General α-glucosidase inhibition assay using α-glucosidase from S. cerevisiae and B. stearothermophilus 16 1.3.5. α-amylase assay 17 1.3.6. Protease assay 17 1.3.7. Cellulase assay 17 1.3.8. Stability of inhibitor measurement 18 1.3.9. Polyphenol measurement 18 1.3.10.Total sugar measurement 18 1.4. Conclusions 18 Chapter 2. Porcine pancreatic α–amylase inhibitors from Euonymus laxiflorus Champ 21 2.1. Introduction 21 2.2. Results and Discussion 22 VI 2.2.1. Screening and evaluation of α-amylase inhibition 22 2.2.2. The pre-incubation time and dialyzing experiment 22 2.2.3. The thermal and pH stabilities of the ELC extract 24 2.2.4. Inhibitory activity of the ELC extract against some α-amylases 26 2.2.5. The influence of reaction time on the inhibitory activity of the extract against some α-amylases 27 2.3. Experimental Section 28 2.3.1. Materials 28 2.3.2. Extraction method 28 2.3.3. Assay of α–amylase inhibitory activity (general assay) 29 2.3.4. Optimal pre–incubation time 29 2.3.5. Stability of inhibitor measurement 29 2.3.6. Statistics 30 2.4. Conclusions 30 Chapter 3. Isolation and identification of novel α-amylase inhibitors from Euonymus laxiflorus Champ 32 3.1. Introduction 32 3.2. Results and Discussion 33 3.2.1. Isolation and purification of active compounds 33 3.2.1.1. Activity of factions after fractionating by Diaion open column 33 3.2.1.2. Activity of sub-factions after sub-fractionating by ODS open column 33 3.2.2. Primary evalution of aAI (%) of isolated compounds and identification of active compounds 37 3.2.3. Inhibitory activity comparison of isolated aAIs and some relationships between chemical structures and bioactivity 41 3.3. Experimental 42 3.3.1 Materials 42 3.3.2 Biological activities and total phenolic acid assays 42 3.3.3 General process of active compounds isolation 42 3.3.4. The HPLC analysis of ELC, ELC3 and Poly Condensed tannin 43 3.4. Conclusions 43 Chapter 4. Biosynthesis of α-glucosidase Inhibitors by a newly isolated bacterium, Paenibacillus sp. TKU042 and its effect on reducing plasma glucose in a mouse model 47 4.1. Introduction 47 4.2. Results and discussion 47 VII 4.2.1. Isolation, screening, and identification of strain TKU042 48 4.2.2. Effects of the C/N (Carbon/Nitrogen) source on aGIs production 49 4.2.3. Optimization of culture condition 50 4.2.4. Specific αGI activity and antioxidant activity of FNB 51 4.2.5. Confirmation that aGIs contained in FNB were produced during NB fermentation 53 4.2.6. The thermal and pH stabilities of FNB aGIs 53 4.2.7. The effects of FNB on reducing plasma glucose in the mouse model 54 4.3. Materials and methods 56 4.3.1. Materials 56 4.3.2. Measurement of rat α-glucosidase inhibition 56 4.3.3. DPPH radical scavenging activity assay 57 4.3.4. Isolation and screening of aGI-producing strains 57 4.3.5. Optimization of culture conditions for synthesis of aGIs 57 4.3.6. Measurement of inhibitor stability 58 4.3.7. Experimental animal protocol 58 4.4. Conclusions 58 Appendix Appendix 1: List of publications during PhD program (2014-2017) 62 Appendix 2: Figure 1. Eunonymus laxiflorus Champ Figure 2. αAIs isolated from Eunonymus laxiflorus Champ 63 Appendix 3: NMR spectrums of Compound 1 64 Appendix 4: NMR spectrums of Compound 10 71 Appendix 5: NMR spectrums of Compound 11 78 VIII List of tables Introduction Page Table 1. Alpha-glucosidase inhibitor and antioxidant conpounds/extracts obtained by microbial convers 4 Chapter 1. Screening and evaluation of α-glucosidase inhibitors from indigenous medicinal plants in Dak Lak Province, Vietnam Table 1. The IC50 values of α-glucosidase inhibitory activities of some Vietnamese medicinal plants 10 Table 2. Alpha-glucosidase inhibition, OD280nm, polyphenol and total sugar concentration (μg) of the ELC extracta before and after dialysis 11 Table 3. IC50 values and maximum inhibitory activity of the ELC extract against some enzymes 14 Chapter 2. Porcine pancreatic α–amylase inhibitors from Euonymus laxiflorus Champ Table 1. The IC50 values of the porcine pancreatic α-amylase inhibitory activity of some Vietnamese medicinal plants 23 Table 2. Porcine pancreatic α-amylase and rat α-glucosidase inhibition by the ELC extracta before and after dialysis 24 Table 3. The thermal stabilities of the ELC extract 25 Table 4. The IC50 and maximum inhibitory activity of the ELC extract against some amylases 26 Chapter 3. Isolation and identification of a novel α-amylase inhibitors from Euonymus laxiflorus Champ Table 1. Alpha-amylase inhibitory activity of ELC and its fractions 34 Table 2. Alpha-amylase inhibitory activity of ELC2, ELC3 and their subfractions 35 Table 3. Alpha-amylase inhibitory activity of isolated aAIs 42 Chapter 4. Biosynthesis of α-Glucosidase Inhibitors by a Newly Isolated Bacterium, Paenibacillus sp. TKU042 and Its Effect on Reducing Plasma Glucose in a Mouse Model Table 1. Comparison of culture conditions before and after optimization 51 Table 2. Specific inhibitory activity of FNB and acarbose against enzymes. 52 IX List of figures Introduction Page Figure 1. The oral a-glucosidase inhibitors currently in clinical use for the treatment of diabetes mellitus. 2 Chapter 1. Screening and evaluation of α-glucosidase inhibitors from indigenous medicinal plants in Dak Lak Province, Vietnam Figure 1. Alpha-glucosidase inhibition activity of the ELC extract 11 Figure 2. pH stability of the ELC extract 12 Figure 3. The thermal stability of ELC extract. 13 Figure 4. Inhibitory activity (%) of the ELC extract against some enzymes 14 Figure 5. The influence of reaction time on the inhibitory activity of the extract against some enzymes 15 Chapter 2. Porcine pancreatic α–amylase inhibitors from Euonymus laxiflorus Champ Figure 1. The pre-incubation time experimental results 24 Figure 2. The pH stability of the ELC extract 26 Figure 3. The inhibitory activity (%) of the ELC extract against some α-amylases 27 Figure 4. The influence of reaction time on the inhibitory activity of the ELC extract against some α-amylases 28 Chapter 3. Isolation and identification of a novel α-amylase inhibitors from Euonymus laxiflorus Champ Figure 1. The isolation chart of active compounds from ELC extract 36 Figure 2. Evalution of aAI (%) of the isolated compounds 37 Figure 3. Chemical structures of isolated inhibitors from ELC extract (A), Key correlations of HMBC and COSY of 3 new compounds (B) 39 Figure 4. HPLC finger print (A) and 13C NMR spectrum (B) of PCT-ELC.3.1-d 40 Chapter 4. Biosynthesis of α-Glucosidase Inhibitors by a Newly Isolated Bacterium, Paenibacillus sp. TKU042 and Its Effect on Reducing Plasma Glucose in a Mouse Model Figure 1. Screening C/N sources for fermentation 49 Figure 2. The effects of some parameters on aGIs production 50 Figure 3. The HPLC finger prints of unfermented and fermented NB 53 Figure 4. Thermal and pH stability of FNB 54 Figure 5. Effects of FNB and acarbose, alone or in combination, on the increase in plasma glucose levels following oral sucrose loading in ICR mice. 55 |
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