专利检索_ .氧作为受体专利检索_ .氧作为受体专利检索查询

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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	生物体试样中的L-色氨酸分析方法以及用于该方法的试剂盒	CN201280011699.0	2012-03-02	CN103635589B	2016-10-12	浅野泰久; 龟谷将史; 尾仲宏康
本发明公开了一种包括将样品、L‑色氨酸氧化酶和水混合的步骤、将所得反应液在氧的存在下放置指定时间的步骤、测定放置后的反应液中存在的因所述酶的作用而产生的反应产物的步骤的L‑色氨酸的定量方法。所述L‑色氨酸氧化酶具有指定氨基酸序列，且具有在氧和水的存在下，作用于L‑色氨酸而生成过氧化氢和氨的氧化酶活性，对L‑苯丙氨酸的氧化酶活性是对L‑色氨酸的氧化酶活性的0～3%的范围，对L‑色氨酸和L‑苯丙氨酸以外的组成蛋白质的氨基酸不具有氧化酶活性。本发明还公开了包含上述L‑色氨酸氧化酶的L‑色氨酸的定量用试剂盒和使用上述L‑色氨酸氧化酶的酶传感器。本发明的方法、试剂盒和酶传感器使用了L‑色氨酸特异性酶，因此即使在其他氨基酸共存下也能对L‑色氨酸进行定量。
2	生物体试样中的L-色氨酸分析方法以及用于该方法的试剂盒	CN201280011699.0	2012-03-02	CN103635589A	2014-03-12	浅野泰久; 龟谷将史; 尾仲宏康
本发明公开了一种包括将样品、L-色氨酸氧化酶和水混合的步骤、将所得反应液在氧的存在下放置指定时间的步骤、测定放置后的反应液中存在的因所述酶的作用而产生的反应产物的步骤的L-色氨酸的定量方法。所述L-色氨酸氧化酶具有指定氨基酸序列，且具有在氧和水的存在下，作用于L-色氨酸而生成过氧化氢和氨的氧化酶活性，对L-苯丙氨酸的氧化酶活性是对L-色氨酸的氧化酶活性的0～3%的范围，对L-色氨酸和L-苯丙氨酸以外的组成蛋白质的氨基酸不具有氧化酶活性。本发明还公开了包含上述L-色氨酸氧化酶的L-色氨酸的定量用试剂盒和使用上述L-色氨酸氧化酶的酶传感器。本发明的方法、试剂盒和酶传感器使用了L-色氨酸特异性酶，因此即使在其他氨基酸共存下也能对L-色氨酸进行定量。
3	MYCOTOXIN-REDUCING COMPOSITION	US14577567	2014-12-19	US20150150285A1	2015-06-04	STEPHEN PHILIP MANN; DAVID PARFITT
A composition comprising an enzyme, a mycotoxin-binding agent and a microorganism capable of taking up a mycotoxin.
4	Mycotoxin-reducing composition	US14577567	2014-12-19	US09901108B2	2018-02-27	Stephen Philip Mann; David Parfitt
A composition comprising an enzyme, a mycotoxin-binding agent and a microorganism capable of taking up a mycotoxin.
5	MYCOTOXIN-REDUCING COMPOSITION	US12447837	2007-11-01	US20110150853A1	2011-06-23	Stephen Philip Mann; David Parfitt
A composition comprising an enzyme, a mycotoxin-binding agent and a microorganism capable of taking up a mycotoxin.
6	Method of Analyzing L-Tryptophan in Biological Samples, and Kit Used Therein	US15608460	2017-05-30	US20170268033A1	2017-09-21	Yasuhisa Asano; Masafumi Kameya; Hiroyasu Onaka
Disclosed is a method for quantifying L-tryptophan involving a step for mixing a specimen, L-tryptophan oxidase, and water, a step for allowing the obtained reaction solution to stand a predetermined period of time in the presence of oxygen, and a step for measuring the reaction product resulting from action of enzymes present in the reaction solution after allowing to stand. The L-tryptophan oxidase has a given amino acid sequence and has oxidase activity that generates hydrogen peroxide and ammonia by acting on the L-tryptophan in the presence of oxygen and water. The oxidase activity of the L-tryptophan oxidase on the L-phenylalanine is in the range of 0-3% of the oxidase activity thereof on the L-tryptophan, and the L-tryptophan oxidase does not have oxidase activity on protein-constituting amino acids other than L-tryptophan and L-phenylalanine. Also disclosed are a kit used to quantify the L-tryptophan containing L-tryptophan oxidase, and an enzyme sensor using the L-tryptophan oxidase. This method, kit and enzyme sensor use an L-tryptophan-specific enzyme, so are capable of quantifying L-tryptophan even in the presence of other amino acids.
7	Method of analyzing L-tryptophan in biological samples, and kit used therein	US14016408	2013-09-03	US09695460B2	2017-07-04	Yasuhisa Asano; Masafumi Kameya; Hiroyasu Onaka
Disclosed is a method for quantifying L-tryptophan involving a step for mixing a specimen, L-tryptophan oxidase, and water, a step for allowing the obtained reaction solution to stand a predetermined period of time in the presence of oxygen, and a step for measuring the reaction product resulting from action of enzymes present in the reaction solution after allowing to stand. Also disclosed are a kit used to quantify the L-tryptophan containing L-tryptophan oxidase, and an enzyme sensor using the L-tryptophan oxidase. This method, kit and enzyme sensor use an L-tryptophan-specific enzyme, so are capable of quantifying L-tryptophan even in the presence of other amino acids.
8	Method of Analyzing L-Tryptophan in Biological Samples, and Kit Used Therein	US14016408	2013-09-03	US20130344526A1	2013-12-26	Yasuhisa Asano; Masafumi Kameya; Hiroyasu Onaka
Disclosed is a method for quantifying L-tryptophan involving a step for mixing a specimen, L-tryptophan oxidase, and water, a step for allowing the obtained reaction solution to stand a predetermined period of time in the presence of oxygen, and a step for measuring the reaction product resulting from action of enzymes present in the reaction solution after allowing to stand. The L-tryptophan oxidase has a given amino acid sequence and has oxidase activity that generates hydrogen peroxide and ammonia by acting on the L-tryptophan in the presence of oxygen and water. The oxidase activity of the L-tryptophan oxidase on the L-phenylalanine is in the range of 0-3% of the oxidase activity thereof on the L-tryptophan, and the L-tryptophan oxidase does not have oxidase activity on protein-constituting amino acids other than L-tryptophan and L-phenylalanine. Also disclosed are a kit used to quantify the L-tryptophan containing L-tryptophan oxidase, and an enzyme sensor using the L-tryptophan oxidase. This method, kit and enzyme sensor use an L-tryptophan-specific enzyme, so are capable of quantifying L-tryptophan even in the presence of other amino acids.
9	In a biological sample l- tryptophan analysis methods and kits to be used in it	JP2012046414	2012-03-02	JP5212996B2	2013-06-19	泰久浅野; 将史亀谷; 宏康尾仲
Disclosed is a method for quantifying L-tryptophan involving a step for mixing a specimen, L-tryptophan oxidase, and water, a step for allowing the obtained reaction solution to stand a predetermined period of time in the presence of oxygen, and a step for measuring the reaction product resulting from action of enzymes present in the reaction solution after allowing to stand. The L-tryptophan oxidase has a given amino acid sequence and has oxidase activity that generates hydrogen peroxide and ammonia by acting on the L-tryptophan in the presence of oxygen and water. The oxidase activity of the L-tryptophan oxidase on the L-phenylalanine is in the range of 0-3% of the oxidase activity thereof on the L-tryptophan, and the L-tryptophan oxidase does not have oxidase activity on protein-constituting amino acids other than L-tryptophan and L-phenylalanine. Also disclosed are a kit used to quantify the L-tryptophan containing L-tryptophan oxidase, and an enzyme sensor using the L-tryptophan oxidase. This method, kit and enzyme sensor use an L-tryptophan-specific enzyme, so are capable of quantifying L-tryptophan even in the presence of other amino acids.
10	Method of analyzing l-tryptophan in biological specimen and kit used for the same	JP2012046414	2012-03-02	JP2012196207A	2012-10-18	ASANO YASUHISA; KAMETANI MASAFUMI; ONAKA HIROYASU
PROBLEM TO BE SOLVED: To provide a method allowing quantity determination of L-tryptophan even under coexistence with another amino acid by use of an L-tryptophan-specific enzyme, and to provide a kit and an enzyme sensor usable for the same.SOLUTION: This method for quantifying L-tryptophan includes steps for: mixing a specimen, L-tryptophan oxidase, and water; leaving the obtained reaction liquid for a prescribed time under the presence of oxygen; and measuring the reaction product by action of the enzyme present in the reaction liquid after the leaving. The L-tryptophan oxidase has a prescribed amino acid sequence, and has oxidase activity generating hydrogen peroxide and ammonia by acting on L-tryptophan under the presence of oxygen and water. The oxidase activity on L-phenylalanine is in the range of 0-3% of the oxidase activity on L-tryptophan, and the L-tryptophan oxidase does not have oxidase activity on protein-constituting amino acids except L-tryptophan and L-phenylalanine. The kit for quantifying L-tryptophan contains the L-tryptophan oxidase. The enzyme sensor uses the L-tryptophan oxidase.
11	MYCOTOXIN-REDUCING COMPOSITION	EP07824430.8	2007-11-01	EP2094107B1	2010-12-29	Mann, Stephen Philip; Parfitt, David
A composition comprising an enzyme, a mycotoxin-binding agent and a microorganism capable of taking up a mycotoxin.
12	MYCOTOXIN-REDUCING COMPOSITION	EP07824430.8	2007-11-01	EP2094107A2	2009-09-02	Mann, Stephen Philip; Parfitt, David
A composition comprising an enzyme, a mycotoxin-binding agent and a microorganism capable of taking up a mycotoxin.
13	생체 시료 중의 L-트립토판 분석 방법 및 그것에 이용하는 키트	KR1020137024100	2012-03-02	KR101916491B1	2018-11-07	아사노야스히사; 가메야마사후미; 오나카히로야스
검체와 L-트립토판옥시다아제와물을혼합하는공정, 얻어진반응액을산소의존재하에서소정시간방치하는공정, 방치후의반응액중에존재하는상기효소의작용에의한반응생성물을계측하는공정을포함하는, L-트립토판의정량방법을개시한다. 상기 L-트립토판옥시다아제는, 소정아미노산서열을가지며, 또한산소및 물의존재하에, L-트립토판에작용하여과산화수소와암모니아를생성하는옥시다아제활성을갖고, L-페닐알라닌에대한옥시다아제활성은 L-트립토판에대한옥시다아제활성의 0∼3%의범위이고, L-트립토판및 L-페닐알라닌이외의단백질구성아미노산에대해서는옥시다아제활성을갖지않는다. 상기 L-트립토판옥시다아제를포함하는 L-트립토판의정량용키트및 상기 L-트립토판옥시다아제를이용하는효소센서도개시한다. 본발명의방법, 키트및 효소센서는, L-트립토판특이적인효소를이용하기때문에, 다른아미노산공존하에서도 L-트립토판을정량할수 있다.
14	생체 시료 중의 L-트립토판 분석 방법 및 그것에 이용하는 키트	KR1020137024100	2012-03-02	KR1020140020273A	2014-02-18	아사노야스히사; 가메야마사후미; 오나카히로야스
검체와 L-트립토판옥시다아제와 물을 혼합하는 공정, 얻어진 반응액을 산소의 존재하에서 소정 시간 방치하는 공정, 방치 후의 반응액 중에 존재하는 상기 효소의 작용에 의한 반응 생성물을 계측하는 공정을 포함하는, L-트립토판의 정량 방법을 개시한다. 상기 L-트립토판옥시다아제는, 소정 아미노산 서열을 가지며, 또한 산소 및 물의 존재하에, L-트립토판에 작용하여 과산화수소와 암모니아를 생성하는 옥시다아제 활성을 갖고, L-페닐알라닌에 대한 옥시다아제 활성은 L-트립토판에 대한 옥시다아제 활성의 0∼3%의 범위이고, L-트립토판 및 L-페닐알라닌 이외의 단백질 구성 아미노산에 대해서는 옥시다아제 활성을 갖지 않는다. 상기 L-트립토판옥시다아제를 포함하는 L-트립토판의 정량용 키트 및 상기 L-트립토판옥시다아제를 이용하는 효소 센서도 개시한다. 본 발명의 방법, 키트 및 효소 센서는, L-트립토판 특이적인 효소를 이용하기 때문에, 다른 아미노산 공존하에서도 L-트립토판을 정량할 수 있다.
15	MYCOTOXIN-REDUCING COMPOSITION	PCT/GB2007004191	2007-11-01	WO2008053232A3	2008-08-21	MANN STEPHEN PHILIP; PARFITT DAVID
A composition comprising an enzyme, a mycotoxin-binding agent and a microorganism capable of taking up a mycotoxin.

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