专利检索_ ..L-谷氨酸氧化酶专利检索_ ..L-谷氨酸氧化酶专利检索查询

序号	专利名	申请号	申请日	公开（公告）号	公开（公告）日	发明人
1	一种高效生产L-谷氨酸氧化酶的方法	CN201510179796.6	2015-04-15	CN104745545A	2015-07-01	刘立明; 樊祥臣; 陈乐乐
本发明公开了一种高效生产L-谷氨酸氧化酶的方法，属于发酵工程和酶工程技术领域。本发明方法中L-谷氨酸氧化酶重组菌最优诱导条件25-30℃，乳糖5g/L诱导5h；通过分批补料发酵不同的补料方式研究，发现采用指数补料和DO-stat相结合的方式有利于菌体密度的增加；通过对分批发酵的诱导条件优化，发现最佳诱导条件为对数期OD600＝40、10g/L乳糖诱导12h，酶活最高达到156.1U/mL；将高表达重组湿菌体添加到含有110g/L的谷氨酸pH8.0的缓冲液中，37℃转化24h可以生产107.9g/L的α-酮戊二酸，转化率达到90％以上，所需菌液量仅为摇瓶发酵的1/50。
2	一种成熟L‑谷氨酸氧化酶的生产方法	CN201611193866.4	2016-12-21	CN106566841A	2017-04-19	唐云平; 丁国芳; 余方苗; 杨最素; 黄芳芳
本发明公开了一种成熟L‑谷氨酸氧化酶的生产方法，首先构建含有L‑谷氨酸氧化酶基因和蛋白酶K基因的重组表达载体pPIC9K‑LGOX和pPICZα‑proteinase K，并依此转化至毕赤酵母GS115中并进行抗性筛选；挑取转化子并利用甲醇进行诱导表达，热处理后通过离心‑硫酸铵沉淀‑离心‑复溶步骤，获得所需的成熟LGOX，本发明利用重组毕赤酵母同时分泌表达LGOX和蛋白酶K，快速获得成熟LGOX，从而降低LGOX的生产成本，以满足α‑酮戊二酸的酶法生产及生物传感器固定化酶膜的制备。
3	NEURO-CHEMICAL SENSOR WITH SELECTIVELY PERMEABLE MEMBRANE ON NANO-ELECTRODE	US15810356	2017-11-13	US20180340204A1	2018-11-29	Steven J. Holmes; Emily R. Kinser; Qinghuang Lin; Nathan P. Marchack; Roy R. Yu
A biosensor includes an array of electrically conductive nanorods formed on a substrate. The nanorods each includes a nanoscale porous coating formed on a surface of the nanorods from silicon dioxide layers. An enzyme coating is bound to the porous coating.
4	L-glutamate oxidase	US10257398	2001-04-19	US07109008B2	2006-09-19	Kenji Inagaki; Jiro Arima; Makoto Ashiuchi; Toshiharu Yagi; Hitoshi Kusakabe
The present invention provides a novel L-glutamate oxidase, a gene encoding the enzyme, and a method for producing the enzyme. By use of a gene encoding the enzyme, L-glutamate oxidase can be readily prepared at low costs through a recombinant DNA technique. The novel L-glutamate oxidase has the following physicochemical properties: (A) action: catalyzing the following reaction: L-glutamic acid+O2+H2O→α-ketoglutaric acid+H2O2+NH3; (B) substrate specificity: being specific to L-glutamic acid; (C) molecular weight and subunit structure: molecular weight as determined through SDS-polyacrylamide gel electrophoresis of 70,000±6,000, molecular weight as determined through gel filtration of 140,000±10,000, and being a dimer formed of the same subunits having a molecular weight of 70,000±6,000; (D) optimum pH: around pH 6.0 to 8.5; (E) heat stability: being stable up to 60° C. at a pH of 7.4 for 30 minutes; and (F) coenzyme: flavin adenine dinucleotide (FAD).
5	L- glutamic acid oxidase	JP2001577486	2001-04-19	JP4002765B2	2007-11-07	年晴八木; 均日下部; 二朗有馬; 賢二稲垣; 誠芦内

6	L-GLUTAMATE OXIDASE	EP01921904.7	2001-04-19	EP1277839A1	2003-01-22	INAGAKI, Kenji; ARIMA, Jiro; ASHIUCHI, Makoto; YAGI, Toshiharu; KUSAKABE, Hitoshi
The present invention provides a novel L-glutamate oxidase, a gene encoding the enzyme, and a method for producing the enzyme. By use of a gene encoding the enzyme, L-glutamate oxidase can be readily prepared at low costs through a recombinant DNA technique. The novel L-glutamate oxidase has the following physicochemical properties: (A) action: catalyzing the following reaction: ${L-glutamic acid + O}_{2} {+ H}_{2} {O → α-ketoglutaric acid + H}_{2} O_{2} {+ NH}_{3};$ (B) substrate specificity: being specific to L-glutamic acid; (C) molecular weight and subunit structure: molecular weight as determined through SDS-polyacrylamide gel electrophoresis of 70,000 ± 6,000, molecular weight as determined through gel filtration of 140,000 ± 10,000, and being a dimer formed of the same subunits having a molecular weight of 70,000 ± 6,000; (D) optimum pH: around pH 6.0 to 8.5; (E) heat stability: being stable up to 60°C at a pH of 7.4 for 30 minutes; and (F) coenzyme: flavin adenine dinucleotide (FAD).
7	NEURO-CHEMICAL SENSOR WITH SELECTIVELY PERMEABLE MEMBRANE ON NANO-ELECTRODE	US15602332	2017-05-23	US20180340203A1	2018-11-29	Steven J. Holmes; Emily R. Kinser; Qinghuang Lin; Nathan P. Marchack; Roy R. Yu
A biosensor includes an array of electrically conductive nanorods formed on a substrate. The nanorods each includes a nanoscale porous coating formed on a surface of the nanorods from silicon dioxide layers. An enzyme coating is bound to the porous coating.
8	L-glutamate oxidase	US11399446	2006-04-07	US20060228790A1	2006-10-12	Kenji Inagaki; Jiro Arima; Makoto Ashiuchi; Toshiharu Yagi; Hitoshi Kusakabe
The present invention provides a novel L-glutamate oxidase, a gene encoding the enzyme, and a method for producing the enzyme. By use of a gene encoding the enzyme, L-glutamate oxidase can be readily prepared at low costs through a recombinant DNA technique. The novel L-glutamate oxidase has the following physicochemical properties: (A) action: catalyzing the following reaction: L-glutamic acid+O2+H2O→α-ketoglutaric acid+H2O2+NH3; (B) substrate specificity: being specific to L-glutamic acid; (C) molecular weight and subunit structure: molecular weight as determined through SDS-polyacrylamide gel electrophoresis of 70,000±6,000, molecular weight as determined through gel filtration of 140,000±10,000, and being a dimer formed of the same subunits having a molecular weight of 70,000±6,000; (D) optimum pH: around pH 6.0 to 8.5; (E) heat stability: being stable up to 60° C. at a pH of 7.4 for 30 minutes; and (F) coenzyme: flavin adenine dinucleotide (FAD).
9	L-glutamate oxidase	US10257398	2003-06-10	US20040091989A1	2004-05-13	Kenji Inagaki; Jiro Arima; Makoto Ashiuchi; Toshiharu Yagi; Hitoshi Kusakabe
The present invention provides a novel L-glutamate oxidase, a gene encoding the enzyme, and a method for producing the enzyme. By use of a gene encoding the enzyme, L-glutamate oxidase can be readily prepared at low costs through a recombinant DNA technique. The novel L-glutamate oxidase has the following physicochemical properties: (A) action: catalyzing the following reaction: L-glutamic acidnullO2nullH2Onullnull-ketoglutaric acidnullH2O2nullNH3; (B) substrate specificity: being specific to L-glutamic acid; (C) molecular weight and subunit structure: molecular weight as determined through SDS-polyacrylamide gel electrophoresis of 70,000null6,000, molecular weight as determined through gel filtration of 140,000null10,000, and being a dimer formed of the same subunits having a molecular weight of 70,000null6,000; (D) optimum pH: around pH 6.0 to 8.5; (E) heat stability: being stable up to 60null C. at a pH of 7.4 for 30 minutes; and (F) coenzyme: flavin adenine dinucleotide (FAD).
10	L-GLUTAMATE OXIDASE	EP01921904.7	2001-04-19	EP1277839B1	2008-02-27	INAGAKI, Kenji; ARIMA, Jiro; ASHIUCHI, Makoto; YAGI, Toshiharu; KUSAKABE, Hitoshi

11	L-GLUTAMATE OXIDASE	EP01921904	2001-04-19	EP1277839A4	2004-05-12	INAGAKI KENJI; ARIMA JIRO; ASHIUCHI MAKOTO; YAGI TOSHIHARU; KUSAKABE HITOSHI
L-Glutamate oxidase having the following physicochemical properties and gene thereof: (A) Function: L-glutamic acid + O2 + H2O → α-ketoglutaric acid + H2O2 + NH3. (B) Substrate specificity: being specific to L-glutamic acid. (C) Molecular weight and subunit structure: molecular weight determined by SDS-polyacrylamide gel electrophoresis: 70000 ± 6000, molecular weight determined by gel filtration: 140000 ± 10000. Being a dimer composed of the same subunits having a molecular weight of 70000 ± 6000. (D) Optimum pH: around pH 6.0 to 8.5. (E) Heat stability: being stable up to 60°C at pH 7.4 for 30 minutes. (F) Coenzyme: flavin adenine dinucleotide (FAD).

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