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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 許輔(Fuu Sheu) | |
| dc.contributor.author | "Chieh-Lun, Ho" | en |
| dc.contributor.author | 何潔倫 | zh_TW |
| dc.date.accessioned | 2021-06-17T03:16:08Z | - |
| dc.date.available | 2021-08-01 | |
| dc.date.copyright | 2018-08-01 | |
| dc.date.issued | 2018 | |
| dc.date.submitted | 2018-07-04 | |
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| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/69454 | - |
| dc.description.abstract | 酶解法是目前產業界常用來提升蛋白質功能性的方法，然而此處理會伴隨苦味胜肽的生成，造成蛋白水解物於食品工業上的應用限制。Aspergillus oryzae 為 GRAS (Generally recognized as safe) 菌種，廣泛使用於東方飲食，可生產改善蛋白質風味的酵素，亦為商業風味蛋白酶 Flavourzyme™ 的生產菌種。本研究選用商業複合酵素 Flavourzyme™ 中的主要酵素— M28 家族中之白胺酸胺基肽酶 A (leucine aminopeptidase A, lapA) ，並且透過 Escherichia coli 異體表現的方式，生產單一重組蛋白，期望純化出單一重組 lapA，可用於改善苦味胜肽的風味。lapA全長為1,134 bp，具337個胺基酸，經預測分析 lapA 為 pre-pro-mature 酵素結構。為確認 pro-peptide 於 lapA的必要性，分別將 pro-mature-peptide (lapAp) 與 mature-peptide (lapAm) 構築至表現載體 pET-22b(+)，並轉形至 E. coli BL21 (DE3)。E. coli BL21 所表現之rHis-lapA 多為不具活性且不可溶之包涵體 (inclusion bodies) 形式，本研究利用尿素回溶包涵體，以親和性管柱進行純化，並透過氧化還原法，成功將rHis-lapAp 復性為具有白胺酸胺基肽酶活性之重組酵素，同時確認 pro-peptide 為蛋白酶形成活性之必要片段。結果顯示 rHis-lapAp 酵素比活性為 2096.02 mU/mg，其最適溫度及最適酸鹼度分別為 50℃ 與pH 6-7，並且於 30℃ 下具有熱穩定性。本研究選殖出之 lapAp 未來可進一步探討是否具改善胜肽苦味之修飾功能，而純化與復性方法可作為 LAPs M28 家族中，以 E. coli 表現胺基肽酶之案例。 | zh_TW |
| dc.description.abstract | Enzymatic hydrolysis has been widely used to improve the functions of protein. However, the enzymatic treatments usually come with the formation of bitter peptides, which seriously limit the application of protein hydrolysates in food industry. Aspergillus oryzae regarded as GRAS (Generally Recognized As Safe) has a long history in the use of fermentation industry in tthe oriental diet. A. oryzae can produce enzymes that reduce the bitterness of hydrolysate. Moreover, commercial complex protease Flavourzyme™ is also derived from A. oryzae. In this study, we chose one of the major enzymes from Flavourzyme™, M28 lapA (leucine aminopeptidase A), as the target. Then lapA gene from A. oryzae ATCC 42149 was cloned and expressed in Escherichia coli system for purifying single recombinant lapA, trying to modify the flavor of protein. Full sequence of lapA was 1,134 bp, and the sequence encoded 378 amino acids residues, which predicted as a pre-pro-mature enzyme. Two truncated lapA, including lapAp (pro-mature peptide) and lapAm (mature peptide), were inserted to the expression vector pET-22b(+) and transformed into E. coli BL21 (DE3) in order to confirm the necessity of pro-peptide. Most of the recombinant rHis-lapA formed as biological inactive inclusion bodies. Hence, urea was used to solubilize inclusion bodies and rHis-lapA was purified by affinity chromatography under denaturing condition. After that, rHis-lapA was refolded and activated successfully by redox method. Meanwhile, we confirmed that pro-peptide was an essential domain for production of active lapA. Renatured rHis-lapAp had a specific activity of 2096.02 mU/mg. It exhibited great stability below 30℃ while optimum temperature and pH was observed at 50℃ and pH 6-7, respectively. This study provided supportive information for future investigation regarding the application to remove bitterness from hydrolysate. Furthermore, the purification and folding treatment of lapAp could be helpful for a better understanding of expressing M28 family LAPs in E. coli. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-17T03:16:08Z (GMT). No. of bitstreams: 1 ntu-107-R05628203-1.pdf: 5505127 bytes, checksum: 7b6fac45b3721c188cc5c6220e7071f2 (MD5) Previous issue date: 2018 | en |
| dc.description.tableofcontents | 口試委員會審定書 i
致謝 ii 摘要 iii Abstract iv 目 錄 vi 表目錄 x 圖目錄 xi 補充資料 xiii 第一章 文獻回顧 1 第一節 胜肽的呈味 1 1.1苦味胜肽 2 第二節 以蛋白酶降低胜肽苦味之應用 3 2.1 酶簡介 3 2.2 蛋白酶簡介 4 2.3 蛋白酶修飾胜肽苦味 5 2.4 市售食品級蛋白酶 6 第三節 米麴菌 (Aspergillus oryzae) 8 第四節 蛋白質表現系統 9 4.1 Escherichia coli 11 4.2 Pichia pastoris 13 第五節 Lap 選殖與表現 14 第二章 研究動機與目的 18 第三章 材料與方法 19 第一節 商業酵素 Flavourzyme™ 分析 21 1.1 Flavourzyme™ 樣品製備 22 1.2 變性膠體製備 22 1.3 膠體電泳、染色與退染 23 第二節 米麴菌白胺酸胺基肽酶基因 (lapA) 之選殖 23 2.1引子 (primer) 設計 23 2.2 米麴菌轉錄體萃取與反轉錄聚合酶鏈鎖反應 24 2.3聚合酶鏈鎖反應 26 2.4 DNA膠體電泳分析 26 2.5 PCR產物純化 26 2.6 TA cloning 及藍白篩 27 2.7 定序分析 27 2.8 質體DNA製備 28 2.9 構築質體 pETLm、pETLp、pICLm 28 2.10 膠體純化限制酶處理片段 29 2.11 接合反應 29 2.12 DNA濃度測定 30 第三節 重組蛋白 rHis-lapA 表現 30 3.1 Escherchia coli 菌株培養與融合蛋白之表現 30 第四節 重組蛋白 rHis-lapA 純化 31 4.1 FPLC系統純化酵素粗萃上清液之rHis-lapA 32 4.1 FPLC系統純化包涵體粗萃液之rHis-lapA 32 4.3 蛋白濃度測定nano-drop 33 第五節 濕式轉印及西方墨點轉漬法 33 5.1 濕式轉印 34 5.2 西方墨點轉漬法 34 第六節 蛋白酶活性分析 Leu-pNA assay 34 6.1 蛋白質濃度測定 35 6.2 p-nitroaniline標準曲線繪製 35 6.3 酵素呈色法 35 第七節 重組蛋白 rHis-lapA 復性 35 7.1 尿素透析復性法 36 7.2 SDS 沉澱復性法 37 7.3 鋅離子共培養復性法 37 7.4 氧化還原復性法 37 第八節 重組蛋白 rHis-lapA 之生化特性分析 38 8.1 最適反應溫度 38 8.2 最適反應 pH 值 38 8.3 溫度安定性 39 第九節 膠體內水解 39 第四章 研究結果 41 第一節 商業酵素 Flavourzyme™ 分析 41 第二節 白胺酸胺基肽酶基因選殖 41 第三節 表現載體之構築及重組蛋白之生產 44 第四節 重組蛋白 rHis-LapA 純化 46 第五節 尿素法純化重組蛋白 rHis-LapA 與復性 46 第六節 重組蛋白 rHis-lapA 之生化特性分析 48 第七節 活性 rHis-lapA 之序列與位置 48 第五章 討論 50 第一節 Flavourzyme 50 第二節 白胺酸胺基肽酶基因選殖 51 第三節 rHis-lapA 表現與酵素活性 52 第四節 rHis-lapA 純化 54 第五節 rHis-lapA 復性 55 5.1 尿素透析復性法 55 5.2 SDS 沉澱復性法 55 5.3 鋅離子共培養復性法 56 5.4 氧化還原復性法 56 第六節 rHis-lapA 之生化特性 57 第七節 pro-peptide 之於酵素活性的重要性 58 第六章 結論與未來展望 60 參考文獻 61 | |
| dc.language.iso | zh-TW | |
| dc.subject | Flavourzyme | zh_TW |
| dc.subject | 米麴? | zh_TW |
| dc.subject | 白胺酸胺基?? | zh_TW |
| dc.subject | M28 LAPs | zh_TW |
| dc.subject | pro-peptide | zh_TW |
| dc.subject | 包涵體 | zh_TW |
| dc.subject | 復性 | zh_TW |
| dc.subject | inclusion bodies | en |
| dc.subject | Flavourzyme | en |
| dc.subject | Aspergillus oryzae | en |
| dc.subject | leucine aminopeptidase | en |
| dc.subject | M28 LAPs | en |
| dc.subject | pro-peptide | en |
| dc.subject | refolding | en |
| dc.title | 米麴菌白胺酸胺基肽酶之選殖、表現與胞外復性 | zh_TW |
| dc.title | Molecular Cloning, Gene Expression and in vitro
Renaturation of a Recombinant Leucine Aminopeptidase from Aspergillus oryzae | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 106-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 蘇南維,周志輝,繆希椿 | |
| dc.subject.keyword | Flavourzyme,米麴?,白胺酸胺基??,M28 LAPs,pro-peptide,包涵體,復性, | zh_TW |
| dc.subject.keyword | Flavourzyme,Aspergillus oryzae,leucine aminopeptidase,M28 LAPs,pro-peptide,inclusion bodies,refolding, | en |
| dc.relation.page | 117 | |
| dc.identifier.doi | 10.6342/NTU201801292 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2018-07-05 | |
| dc.contributor.author-college | 生物資源暨農學院 | zh_TW |
| dc.contributor.author-dept | 園藝暨景觀學系 | zh_TW |
| 顯示於系所單位： | 園藝暨景觀學系 | |
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