Development of superbioreactors

超级生物反应器的开发

• 批准号: 03555179
• 负责人: KONDO Hiroki
• 金额: $ 9.47万
• 依托单位: Kyushu Institute of Technology
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Developmental Scientific Research (B)
• 财政年份: 1991
• 资助国家: 日本
• 起止时间: 1991 至 1992
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-03555179/
• 关键词: organic solvent systems; chemical modification of enzymes; lipases; conversion of enzyme functions; organic silicon compounds; stereoselective esterification; support-free bioreactors; tubular; 酵素機能交換; リパ-ゼ; 光学分割; テルペンアルコ-ル; 2-(4-クロロフェノキシ)プロピオ

A.Development of catalytic devices (1)Conversion of enzyme functions by chemical modification: Upon chemical modification of tyrosine residues of a Pseudomonaslipase, its esterase activity was reduced drastically, while lipase activity was little affected. This phenomenon was observed when two of the tyrosine residues of this enzyme were modified. (2) Search of biocatalysts effective for transformation of unnatural compounds: Enzymatic optical resolution of 2-trimethylsily(TMS)-1- propanol(A),1-TMS-2-propanol(B) and 1-TMS-1-propanol(C) was attempted. Unlike chemical methods, enzymatic methods were found to be superior for esterifying A and B with 5-phenylvaleric acid. Furthermore, efficient optical resolution was achieved for B with Pseudomonas sp. lipoprotein lipase. Because of a steric bulk, C reacted more slowly than A and B. but a significant stereoselectivity was observed for C as well.B.Development of support-free biocatalystStereoselective esterification of dl-2-(4-chlorophenoxy) propionic acid with myristyl alcohol was carried out in water-saturated carbon tetrachloride-issoctanol (8:2) in the presence of yeast lipase OF360 at 30ﾟC. A 3-fold higher rate and high stereoselectivity was observed for enzyme powder than that for celite-adsorbed enzyme. As an application a continuous reactor was developed in which a glass column was filled with enzyme powder. This system yielded a 4-fold higher productivity than the celite-adsorbed enzyme.

A.催化装置的开发（1）通过化学修饰实现酶功能的转化：在对假单胞菌脂肪酶的酪氨酸残基进行化学修饰后，其酯酶活性急剧降低，而脂肪酶活性几乎不受影响。当这种酶的两个酪氨酸残基被修饰时，观察到这种现象。(2)寻找有效转化非天然化合物的生物催化剂：尝试了2-三甲基硅基（TMS）-1-丙醇（A）、1-TMS-2-丙醇（B）和1-TMS-1-丙醇（C）的酶促光学拆分。与化学方法不同，发现酶促方法对于用5-苯基戊酸纯化A和B是上级的。利用假单胞菌脂蛋白脂肪酶对B进行了高效的光学拆分。由于空间位阻，C的反应比A和B慢。B.无载体生物催化剂的开发在水饱和的四氯化碳-异辛醇（8：2）中，在酵母脂肪酶OF 360的存在下，在30 ℃下进行dl-2-（4-氯苯氧基）丙酸与肉豆蔻醇的立体选择性酯化。酶粉比硅藻土吸附的酶有高3倍的反应速率和高的立体选择性。作为应用，开发了连续反应器，其中玻璃柱填充有酶粉。该系统产生了比硅藻土吸附的酶高4倍的生产率。

项目成果

Masaya Kawase: "Inspcction of an acyl-enzyme intermediate in a lipase reaction by gas Chromatography-mass spcctrometry and modeling of the reaction mechanism." Biocatalysis. 6. 43-50 (1992)

Masaya Kawase：“通过气相色谱-质谱法检查脂肪酶反应中的酰基酶中间体以及反应机制的建模。”

Shigeori TAKENAKA: "Synthesis and characterization of novel tris-intercalators having potentially two different DNA binding modes." Supramol.Chem.(1993)

Shigeori TAKENAKA：“具有两种不同 DNA 结合模式的新型三嵌入剂的合成和表征。”

Masaya Kawase et al.: "Inspection of an acyl-enzyme intermediate in a lipase reaction by gas chromatography-mass spectrometry and modeling of the reaction mechanism,Biocatalysis" 6,43 (1992)

Masaya Kawase 等人：“通过气相色谱-质谱法检查脂肪酶反应中的酰基酶中间体以及反应机理建模，生物催化”6,43 (1992)

Masaya KAWASE: "Inspection of an acyl-enzyme intermediate in a lipase reaction by gas chromatography-mass spectrometry and modeling of the reaction mechanism." Biocatalysis. 6. 43-50 (1992)

Masaya KAWASE：“通过气相色谱-质谱法检查脂肪酶反应中的酰基酶中间体并建模反应机制。”

Shigeori Takenaka: "Synthesis and characterization of novel tris intercalators having potentially two different DNA binding modes." Supramol.Chem.(1993)

Shigeori Takenaka：“具有两种不同 DNA 结合模式的新型 tris 嵌入剂的合成和表征。”