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일반 설명
Monellin is considered a sweet protein and consists of two subunits, chain A and chain B. It is used as a non-carbohydrate sweetener and is beneficial for diabetic patients.
애플리케이션
Monellin from Dioscoreophyllum cumminsii (serendipity berry) has been used in biophysical studies.
기타 정보
An intensely sweet protein.
품질
Partially purified.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
Nilesh Aghera et al.
Protein expression and purification, 76(2), 248-253 (2010-11-10)
Monellin is an intensely sweet-tasting protein present in the berry of Dioscoreophyllum cumminsii. Naturally occurring monellin (double chain monellin) is a heterodimer of two subunits commonly referred to as chain A and chain B. Monellin is a good model system
Wei-Feng Xue et al.
Proteins, 57(3), 586-595 (2004-09-24)
Accurate and precise determinations of thermodynamic parameters of binding are important steps toward understanding many biological mechanisms. Here, a multi-method approach to binding analysis is applied and a detailed error analysis is introduced. Using this approach, the binding thermodynamics and
Wei-Feng Xue et al.
Biochimica et biophysica acta, 1794(3), 410-420 (2008-12-23)
A small number of proteins have the unusual property of tasting intensely sweet. Despite many studies aimed at identifying their sweet taste determinants, the molecular basis of protein sweetness is not fully understood. Recent mutational studies of monellin have implicated
Luqiang Jia et al.
PloS one, 12(10), e0184602-e0184602 (2017-10-06)
In heterologous protein productions by P. pastoris, methanol induction is generally initiated when cell concentration reaches very high density. The alternative strategy by initiating methanol induction at lower cells concentration was also reported to be effective in easing DO control
Fushan Liu et al.
Journal of experimental botany, 60(15), 4423-4440 (2009-10-07)
The amylose extender (ae(-)) mutant of maize lacks starch branching enzyme IIb (SBEIIb) activity, resulting in amylopectin with reduced branch point frequency, and longer glucan chains. Recent studies indicate isozymes of soluble starch synthases form high molecular weight complexes with
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