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摘 要：谷氨酸脱羧酶（GAD）是生物体内广泛存在的一种酶，有重要的生理学作用，能专一催化L-谷氨酸裂解生成重要的抑制性神经递质γ-氨基丁酸(γ-aminobutyric acid，简称GABA)。本试验以普通大肠杆菌经过诱变筛选得到一株高产谷氨酸脱羧酶（E.coli GAD）菌株以此为基础，研究该菌株最佳转化条件。对其菌株转化时各种条件的影响研究，实验表明：最佳工艺为培养基镁离子约为0.7g/L、钾离子3 g/L、在PH为4.8、温度在37摄氏度、底物浓度为20g/L、菌体浓度为3g/mL、菌龄为18小时。1g湿菌体可重复转化4次，转化为30（g）GABA。
关键词：谷氨酸脱羧酶；GABA；紫外诱变；转化条件；大肠肝菌；
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关键词：谷氨酸脱羧酶；GABA；紫外诱变；转化条件；大肠肝菌；
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最佳答案
Abstract: Glutamic acid decarboxylase (GAD), which is an extensively growing enzyme with important functions in physiology, can decompose L-glutamic acid and generate an valuable inhibitory neutrotransmitterγ-aminobutyric acid (GABA). This test generates a high- yielding GAD strain by mutagenizing and screening the escherichia colis. It is on the basis of this test to study on the optimal conditions of translation in this strain. The study of all conditions for translation by this strain has shown that the best processing is the culture medium containing 0.7g/L magnesium ions and 3g/L potassium ions, and the substrate concentration is 20g/L, the strain concentration is 3g/mL and the strain age is 18 hours when the pH is 4.8 and temperature is 37℃. 1g wet bacteria can repeatedly be translated into 30g GABA, totally for 4 times.
Keywords: Glutamic acid decarboxylase; GABA; UV-mutation; translation condition; escherichia coli
提问者对于答案的评价：谢谢··
Keywords: Glutamic acid decarboxylase; GABA; UV-mutation; translation condition; escherichia coli
2008-6-2 10:09:56
回答者：emersonlee
提问者对于答案的评价：谢谢··
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Abstract: The glutanic acid decarboxylase (GAD) is in organism the widespread existence one kind of enzyme, has the important physiology function, can catalyze the L- glutanic acid decomposition production important suppressant nerve to hand over the nature Gamma - amino-butyric acid single-mindedly (γ-aminobutyric acid, is called GABA). This experiment obtains high production glutanic acid decarboxylase take the ordinary backwoods coli after mutafacient screening (E.coli GAD) the strain by this as a foundation, studies this strain best transformation condition. To its strain transformation when each kind of condition's influence research, the experiment indicated: The best craft is the culture medium magnesium ion approximately is 0.7g/L, potassium ion 3 g/L, in PH is 4.8, temperatures in 37 degrees Celsius, the substrate concentration is 20g/L, the mycelium density is 3g/mL, the cell age is 18 hours. the 1g wet mycelium may duplicate transforms 4 times, the transformation is 30 (g) GABA. とります 要します：グルタミン酸がカルボキシルの酵素（GAD）を脱ぐのは生物の体内の広範な存在の1種の酵素で、重要な生理学の作用があって、一心な促進L-グルタミン酸の分裂分解は重要な抑える性神経を形成して質にγ-をアミノ基の酪酸(γ-aminobutyric acid、略称GABA)を手渡すことができます。当試験は普通の大腸桿菌で変異を通って1本の生産量が多いグルタミン酸を得てカルボキシルの酵素（のEを脱ぐことをふるい分けます.coli GAD）菌の株はだから基礎で、この菌の株の最優秀転化の条件を研究します。その菌の株に対して時の各種の条件の影響する研究を転化さして、実験は表明しています：最優秀技術は育成基のマグネシウムのイオンおよそ0.7g/L、カリウムのイオンの3です g/L、PHで4.8です、温度が37℃で、底の物の濃度が20g/Lです、菌の体の濃度が3g/mLです、菌が齢18時間です。1gは菌の体が濡れて繰り返し4回転化さすることができて、30（g）GABAに転化します。 关键词： Glutanic acid decarboxylase; GABA; Ultraviolet mutagenesis; Transformed condition; Large intestine liver fungus; グルタミン酸はカルボキシルの酵素を脱ぎます；GABA；紫の外に変異；転化の条件；大腸の肝臓菌； 最后修改于 2008-6-6 22:19:02
Abstract: The glutanic acid decarboxylase (GAD) is in organism the widespread existence one kind of enzyme, has the important physiology function, can catalyze the L- glutanic acid decomposition production important suppressant nerve to hand over the nature Gamma - amino-butyric acid single-mindedly (γ-aminobutyric acid, is called GABA). This experiment obtains high production glutanic acid decarboxylase take the ordinary backwoods coli after mutafacient screening (E.coli GAD) the strain by this as a foundation, studies this strain best transformation condition. To its strain transformation when each kind of condition's influence research, the experiment indicated: The best craft is the culture medium magnesium ion approximately is 0.7g/L, potassium ion 3 g/L, in PH is 4.8, temperatures in 37 degrees Celsius, the substrate concentration is 20g/L, the mycelium density is 3g/mL, the cell age is 18 hours. the 1g wet mycelium may duplicate transforms 4 times, the transformation is 30 (g) GABA. |
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