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Merck
所有图片(2)

主要文件

T7638

Sigma-Aldrich

索马甜 来源于非洲竹芋

别名:

Thaumatin Protein

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About This Item

UNSPSC代码:
12352202
NACRES:
NA.56
价格与库存信息目前不能提供

生物来源

plant (Thaumatococcus daniellii)

表单

powder

分子量

~22 kDa

储存温度

2-8°C

一般描述

奇异果甜蛋白是一种从非洲植物卡特莫夫果(Thaumatococcus daniellii Benth)中提取的超甜蛋白质。这种无毒蛋白是广泛的致病相关蛋白家族(PR5组)的成员。[1][2]奇异果甜蛋白有五种亚型,即奇异果甜蛋白I、II、III、a和b。[3]

应用

来自卡特莫夫果的奇异果甜蛋白用于:
  • 作为阳性对照品/标准品,采用蛋白质印迹法检测转基因小鼠乳中奇异果甜蛋白重组蛋白含量[2]
  • 作为标准品,比较其与自流汁中出现的葡萄素样蛋白(VVTL1)的保留时间,并测定葡萄汁中的病程相关蛋白含量[4]
  • 作为模型蛋白,研究其与游离和连接十钒酸盐的相互作用[5]

生化/生理作用

奇异果甜蛋白是一种零卡路里的甜味剂和风味增强剂,适用于食品工业。它具有抗真菌活性,对植物具有保护作用。奇异果甜蛋白在药剂学中很有用,因为它是一种特殊的低热量膳食成分。[1]
最近有研究表明,翅果竹芋中的奇异果甜蛋白基因在番茄中的过表达导致果实味道变甜,这表明奇异果甜蛋白可用于增强各种食物的味道。 [6]

质量

奇异果甜蛋白 I 和奇异果甜蛋白 II 的混合物,含有微量的其他甜味蛋白。

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Chae Un Kim et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(12), 4596-4600 (2009-03-05)
Polymorphism of water has been extensively studied, but controversy still exists over the phase transition between high-density amorphous (HDA) and low-density amorphous (LDA) ice. We report the phase behavior of HDA ice inside high-pressure cryocooled protein crystals. Using X-ray diffraction
Expression of functional plant sweet protein thaumatin II in the milk of transgenic mice
Lu R, et al.
Food and Bioproducts Processing, 125, 222-227 (2021)
Aleksey Firsov et al.
Protein expression and purification, 123, 1-5 (2016-03-12)
Thaumatin, a supersweet protein from the African plant katemfe (Thaumatococcus daniellii Benth.), is a promising zero-calorie sweetener for use in the food and pharmaceutical industries. Due to limited natural sources of thaumatin, its production using transgenic plants is an advantageous
Tuning the interactions of decavanadate with thaumatin, lysozyme, proteinase K and human serum proteins by its coordination to a pentaaquacobalt (ii) complex cation
Krivosudsky L, et al.
New. J. Chem., 43(45), 17863-17871 (2019)
Tetsuya Masuda et al.
Journal of bioscience and bioengineering, 102(5), 375-389 (2006-12-26)
Most proteins are tasteless and flavorless, while some proteins elicit a sweet-taste response on the human palate. Six proteins, thaumatin, monellin, mabinlin, brazzein, egg lysozyme, and neoculin (previously considered as curculin) have been identified as sweet-tasting proteins. However, no common

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