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Merck

40452

Sigma-Aldrich

漆酶 来源于双孢蘑菇

greener alternative

powder, deep brown, ≥4 U/mg

别名:

Uroshiol oxidase

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About This Item

CAS号:
EC號碼:
MDL號碼:
分類程式碼代碼:
12352204

生物源

fungus (Agaricus bisporus)

形狀

powder

比活性

≥4 U/mg

環保替代產品特色

Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

顏色

deep brown

環保替代類別

運輸包裝

wet ice

儲存溫度

−20°C

InChI

1S/C9H13NO/c1-4-10-7(2)5-9(6-11)8(10)3/h5-6H,4H2,1-3H3

InChI 密鑰

NWDZDFOKSUDVJV-UHFFFAOYSA-N

一般說明

我们致力于为您提供更环保的替代产品,以符合“绿色化学的12项原则”的一项或多项原则要求。本品已用作替代能源用酶。更多信息请参阅替代能源研究用酶

應用

漆酶是一种存在于多种植物、真菌和微生物中的多酚氧化酶。漆酶可用于酶生物燃料系统、牙齿美白、纺织品染色和其他需要去除氧气的应用

生化/生理作用

漆酶是一种蓝色的铜氧化酶,可将分子氧还原成水。漆酶可氧化多酚、甲氧基取代的酚和二胺,但不氧化酪氨酸。漆酶的氧化作用是单电子反应,产生自由基

單位定義

1u 相当于在 pH 6.0,25°C 下每分钟转化 1 μmol 邻苯二酚的酶量

象形圖

Health hazard

訊號詞

Danger

危險聲明

防範說明

危險分類

Resp. Sens. 1

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 1

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


分析证书(COA)

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Applications of oxidoreductases: Recent progress.
Xu, Feng
Industrial Biotechnology (New Rochelle, N.Y.), 1, 38-50 (2005)
The structure and function of fungal laccases
Christopher F. Thurston
Microbiology, 140, 19-26 (1994)
Ian R Wheeldon et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(40), 15275-15280 (2008-10-01)
Here, we present two bifunctional protein building blocks that coassemble to form a bioelectrocatalytic hydrogel that catalyzes the reduction of dioxygen to water. One building block, a metallopolypeptide based on a previously designed triblock polypeptide, is electron-conducting. A second building
Meng-Hsuan Wu et al.
Scientific reports, 9(1), 9754-9754 (2019-07-07)
Laccases that are tolerant to organic solvents are powerful bio-catalysts with broad applications in biotechnology. Most of these uses must be accomplished at high concentration of organic solvents, during which proteins undergo unfolding, thereby losing enzyme activity. Here we show
Shanfa Lu et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(26), 10848-10853 (2013-06-12)
Laccases, as early as 1959, were proposed to catalyze the oxidative polymerization of monolignols. Genetic evidence in support of this hypothesis has been elusive due to functional redundancy of laccase genes. An Arabidopsis double mutant demonstrated the involvement of laccases

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