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研究生:林文澤
研究生(外文):Lin, Wenze
論文名稱:綠竹筍重組幾丁質酶催化特性及固定化研究
論文名稱(外文):Studies On The Catalytic Characteristics And Immobilization Of Bamboo Recombinant Chitinase
指導教授:張珍田張珍田引用關係
指導教授(外文):Chang, Chentien
口試委員:張珍田鍾雲琴宋賢一賴麗旭
口試委員(外文):Chang, ChentienChung, YunchinSung, ShianyiLai, Lishiu
口試日期:2012-07-18
學位類別:碩士
校院名稱:靜宜大學
系所名稱:食品營養學系
學門:醫藥衛生學門
學類:營養學類
論文種類:學術論文
論文出版年:2012
畢業學年度:100
語文別:中文
論文頁數:156
中文關鍵詞:幾丁質酶固定化酵素
外文關鍵詞:chitinaseimmobilizanenzyme
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本研究由帶有綠竹筍第三類型幾丁質酶cDNA 之甲醇酵母培養液經由硫酸銨劃分(50-70% saturation)、Sephacryl S-100 HR膠體過濾層析、Rotofor cell製備式等電焦集電泳、Phenyl-Sepharose 6 Fast Flow疏水性層析及Con A-Sepharose 4B親和性層析等連續純化步驟,獲得兩種重組幾丁質酶異構酶A和B,以SDS-PAGE電泳及活性染色測得異構酶A和B之分子量分別為36.1 kDa及30.8 kDa,以pNP-β-GlcNAc4為基質,測得異構酶A和B之最適pH 為3-4;異構酶A之動力學參數Vmax和 Km 為8.36 mole pNP min-1mg-1和3.89 mg/mL;異構酶B之動力學參數Vmax和 Km 為0.87 mole pNP min-1mg-1和0.48 mg/mL。以Dixon-Webb作圖 (log VmH+/KmH+ versus pH 和log VmH+ versus pH ) 分析,顯示二異構酶活性中心有兩個質子可解離基團參與基質之結合及轉換,此二基團之pKa 為pH 2.9-3.1及pH 4.5-5.0。二異構酶亦可水解幾丁聚醣,水解產物主要為低分子量幾丁聚醣 (12.6 kDa-44.6 kDa) 。
純化之異構酶A和B可固定於經戊二醛活化之磁性Fe3O4奈米粒子,固定化後二異構酶水解乙二醇幾丁質之最適pH (pH 3-4) 並未改變,但最適溫度顯著增加,固定化可顯著增加酵素分子之熱穩定性。二固定化異構酶亦可降解幾丁聚醣,在低分子量幾丁聚醣製備上具有應用潛力。

In this study, two recombinant class Ⅲ chitinase isoforms A and B of bamboo shoots were purified from the culture medium of recombinant Pichia pastoria X-33 by following sequential steps of ammonium sulfate fractionation (50-70% saturation), Sephacryl S-100 HR gel filtration, Rotofor cell preparative isoelectric focusing electrophoresis, Phenyl-Sepharose hydrophobic chromatography and Con A-Sepharose chromatography. The molecular masses of isoforms A and B were 36.1 kDa and 30.8 kDa , respectively, as estimated by SDS-PAGE and activity staining. Using pNP-β-GlcNAc4 as the substrate, the optimal pH for the activities of isoforms A and B were pH 3-4. The kinetic parameters Vmax and Km for isoform A were 8.36 mole pNP min-1mg-1 and 3.89 mg/mL, respectively; for isoform B, the kineic parameters were 0.87 pNP min-1mg-1 and 0.48 mg/mL, respectively. Two prototropic groups with pKa values of 2.9-3.1 and 4.5-5 on the active site of both isoforms may be involved in substrate binding and transformation, as examined by Dixon-Webb plots (log VmH+/KmH+ versus pH and log VmH+ versus pH ). Both isoforms could also degrade chitosan. The products of the hydrolysis catalyzed by both isoforms were low molecular chitosan polymers (12.6 kDa-44.6 kDa).
The purified isoforms A and B could be immobilized on glutaraldehyde-activated magnetic Fe3O4 nanoparticles. After immobilization, the optimal pH (pH 3-4) of both isoforms for glycol chitin hydrolysis were unchanged ; but the optimal temperatures were significantly increased. Immobilization significantly increased the thermal stability of both isoforms. Both immobilized isoforms also degrade chitosan polymer and would be useful in producing low molecular weight chitosan.
目錄 I
表目錄 V
圖目錄 VI
縮寫表 X
中文摘要 XII
英文摘要 XIV
第一章 前言 1
第一節 研究背景及目的 1
第二章 文獻回顧 9
第一節 幾丁質水解酵素 9
第二節 微生物之幾丁質酶 26
第三節 幾丁質酶之應用 29
第四節 酵素固定化 32
第三章 材料與方法 48
第一節 實驗材料 48
壹、 化學藥品 48
貳、 重要儀器及器材 49
第二節 實驗方法 50
壹、 酵素活性測定 50
貳、 還原糖校正曲線 52
參、蛋白質定量 53
肆、 胺基醣之MBTH呈色定量 55
伍、 Glycol chitin之製備 56
陸、 磁性奈米粒子的製備 58
柒、 表面含有醛基的磁性奈米粒子製備 61
捌、 重組幾丁質酶純化 64
玖、 重組幾丁質酶性質測定 68
壹拾、 重組幾丁質酶A和B的固定化 73
第四章 結果與討論 77
第一節 第三類型重組幾丁質酶之純化 77
第二節 重組幾丁質酶之性質 83
壹、 純化異構酶A和B之酵素性質 83
一、 SDS-聚丙烯醯胺膠體電泳 83
二、 水解乙二醇幾丁質之酵素動力學 85
三、 pH穩定性 87
四、 儲存穩定性 89
五、 水解pNP-β-GlcNAc4之最適pH 91
六、 pNP-β-GlcNAc4之動力學參數 93
七、 pH對動力學參數 (KmH+及VmaxH+) 之影響 95
貳、 幾丁聚醣水解產物 99
一、 分子量較正曲線 99
二、 幾丁聚醣之產物分子量分布 99
第三節 固定化重組幾丁質酶之製備與性質 104
壹、 固定化重組幾丁質酶製備 104
一、 固定化反應時間對固定化百分率之影響 104
貳、 固定化重組幾丁質酶之性質 107
一、 最適pH值 107
二、 最適溫度 109
三、 熱穩定性 111
四、 動力學參數(Vmax及Km) 114
五、 水解pNP-β-GlcNAc1-5之動力學 117
六、 固定化酵素水解幾丁聚醣之產物分子量分布 120
七、 重複使用性 123
八、 儲存穩定性 125
第五章 結論 127
第六章 未來展望 129
第七章 參考文獻 130
附錄一、 還原糖定量法(neocuproine法) 146
附錄二、 BCA蛋白質定量校正曲線 150
附錄三、 Micro BCA蛋白質定量校正曲線 151
附錄四、 SDS-聚丙烯醯胺膠體電泳標準蛋白質較正曲線 152
附錄五、 磁性奈米微粒固定化幾丁質酶之酵素量與反應速率關係圖 153
附錄六、 pNP-β-GlcNAcn之水解動力學測定 154
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