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      Monellin, a sweet protein, was discovered in 1969 in the fruit of the West African shrub known as serendipity berry (Dioscoreophyllum cumminsii); it was first reported as a carbohydrate. The protein was named in 1972 after the Monell Chemical Senses Center in Philadelphia, U.S.A., where it was isolated and characterized.


      Protein composition


      Monellin's molecular weight is 10.7 kDa. It has two noncovalently associated polypeptide chains: an A chain sequence with 44 amino acid residues, and a B chain with 50 residues.

      Monellin chain A (44 AA):
      REIKGYEYQL YVYASDKLFR ADISEDYKTR GRKLLRFNGP VPPP
      Monellin chain B (50 AA):
      GEWEIIDIGP FTQNLGKFAV DEENKIGQYG RLTFNKVIRP CMKKTIYEEN

      Amino acid sequence of the sweet protein monellin adapted from Swiss-Prot biological database of protein.
      Monellin has a secondary structure consisting of five beta-strands that form an antiparallel beta-sheet and a 17-residue alpha-helix.
      In its natural form, monellin is composed of the two chains shown above (PDB: 3MON​), but the protein is unstable at high temperatures or at extremes of pH. To enhance its stability, single-chain monellin proteins were created in which the two natural chains are joined via a Gly-Phe dipeptide linker. This modified version of the protein (MNEI) has been studied using NMR and X-ray diffraction.
      In addition to its secondary structure, four stably bound sulfate ions were located on the monellin protein, three on the concave face of the protein and one on the convex face of the protein. The sulfate ion on the convex face of the protein is of particular interest because it lies adjacent to a patch of positive surface potential, which may be important in electrostatic interactions with the negative T1R2-T1R3 sweet taste protein receptor.


      Sweetness properties


      Monellin is perceived as sweet by humans and some Old World primates, but is not preferred by other mammals. The relative sweetness of monellin varies from 800 to 2000 times sweeter than sucrose, depending on the sweet reference against which it is assessed. It is reported to be 1500-2000 times sweeter than a 7% sucrose solution on a weight basis
      and 800 times sweeter than sucrose when compared with a 5% sucrose solution on a weight basis.
      Monellin has a slow onset of sweetness and lingering aftertaste. Like miraculin, monellin's sweetness is pH-dependent; the protein is tasteless below pH 2 and above pH 9. Blending the sweet protein with bulk and/or intense sweeteners reduces the persistent sweetness and shows a synergistic sweet effect. Heat over 50 °C at low pH denatures monellin proteins, causing a loss of the sweetness.
      So far, five high-intensity sweet proteins have been reported: monellin (1969), thaumatin (1972), pentadin (1989), mabinlin (1983) and brazzein (1994).


      = As a sweetener

      =
      Monellin can be useful for sweetening some foods and drinks, as it is a protein readily soluble in water due to its hydrophilic properties. However, it may have limited application because it denatures under high temperature conditions, which makes it unsuitable for processed food. It may be relevant as noncarbohydrate tabletop sweetener, especially for individuals such as diabetics who must control their sugar intake.
      In addition, monellin is costly to extract from the fruit and the plant is difficult to grow. Alternative production such as chemical synthesis and expression in micro-organisms are being investigated. For instance, monellin has been expressed successfully in yeast (Candida utilis) and synthesised by solid-phase method. The synthetic monellin produce by yeast was found to be 4000 times sweeter than sucrose when compared to 0.6% sugar solution.
      Legal issues are the main barrier in its widespread use as a sweetener, as monellin has no legal status in the European Union or the United States. However, it is approved in Japan as a harmless additive, according to the List of Existing Food Additives issued by the Ministry of Health and Welfare (published in English by JETRO).


      See also


      Curculin
      Thaumatin
      Miraculin
      Stevia


      References




      External links


      Media related to Monellin at Wikimedia Commons
      Monellin, PDB Molecule of the Month
      Overview of all the structural information available in the PDB for UniProt: P02881 (Monellin chain A) at the PDBe-KB.
      Overview of all the structural information available in the PDB for UniProt: P02882 (Monellin chain B) at the PDBe-KB.

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    Monellin Images, Monellin Transparent PNG, Free download

    Monellin Images, Monellin Transparent PNG, Free download

    Monellin - Valegård Design

    Monellin - Valegård Design

    Monellin - Valegård Design

    Monellin - Valegård Design

    What is Monellin? Unveiling the Sweet Protein and Its Applications

    What is Monellin? Unveiling the Sweet Protein and Its Applications

    Monellin Production Strains Development - Lifeasible

    Monellin Production Strains Development - Lifeasible

    Monellin Market: Global Industry Analysis and Forecast (2023-2029)

    Monellin Market: Global Industry Analysis and Forecast (2023-2029)

    Structure and sweetness of monellin analogs. | Download Table

    Structure and sweetness of monellin analogs. | Download Table

    Structure and sweetness of monellin analogs. | Download Table

    Structure and sweetness of monellin analogs. | Download Table

    Monellin Market Is Used To Target The Population With Diabetes And ...

    Monellin Market Is Used To Target The Population With Diabetes And ...

    Workflow of in vivo selection of monellin mutants with increased ...

    Workflow of in vivo selection of monellin mutants with increased ...

    Affinity chromatography results: binding between monellin and NAbs ...

    Affinity chromatography results: binding between monellin and NAbs ...

    The structure of monellin derived from X-ray diffraction at a 1.15 Å ...

    The structure of monellin derived from X-ray diffraction at a 1.15 Å ...

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    monellin

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    Monellin - Wikipedia

    Monellin, a sweet protein, was discovered in 1969 in the fruit of the West African shrub known as serendipity berry (Dioscoreophyllum cumminsii); it was first reported as a carbohydrate. [2] . The protein was named in 1972 after the Monell Chemical Senses Center in Philadelphia, U.S.A., where it was isolated and characterized. [3]

    Molecule of the Month: Monellin - RCSB: PDB-101

    Monellin and other supersweet proteins trick our taste receptors. Sweet-tasting and taste-modifying molecules. Sugar tastes sweet for a good reason: it’s a fast and easy source of energy for our cells, so evolution has ensured that we’re happy when we eat it.

    What is Monellin? Unveiling the Sweet Protein and Its Applications

    Aug 3, 2023 · Monellin is a natural sweet protein extracted from the serendipity berry, with a sweetness 1500-2000 times greater than sucrose. The protein’s unique structure of 94 amino acids allows it to interact with taste receptors, providing a sweet sensation.

    Brazzein and monellin: Safe alternatives to sugar, new research …

    Nov 10, 2023 · Monellin and brazzein, artificial small-molecule sweeteners, have been widely used to replace sugar in food due to their high sweetness and potential health benefits. Sweet-tasting proteins...

    Monellin - an overview | ScienceDirect Topics

    Monellin is the sweet-tasting protein isolated from fruits or leaves of Dioscoreophyllum cumminsii (Pradhan et al., 2020). Monellin sweetness power is 3000 times greater than sucrose (Kohmura et al., 1990).

    Sweet-Tasting Natural Proteins Brazzein and Monellin: Safe …

    This article presents the results of a comprehensive toxicity assessment of brazzein and monellin, yeast-produced recombinant sweet-tasting proteins. Excessive sugar consumption is one of the leading dietary and nutritional problems in the world, ...

    Sweeter and stronger: enhancing sweetness and stability of the …

    Sep 23, 2016 · Monellin, isolated from the African plant Dioscoreophyllum cumminsii, is, together with thaumatin, one of the most potent sweeteners known, being about 90,000 times sweeter than sucrose on a...

    Monellin - an overview | ScienceDirect Topics

    Monellin is a plant protein isolated from the fruit of the tropical plant Dioscoreophyllum cumminsii. It is a sweet-tasting protein composed of two subunits, one being 45 residues (A chain) and the other 50 residues (B chain).

    A sweet protein monellin as a non-antibody scaffold for synthetic ...

    Jul 3, 2021 · Here, we describe the first application of a phage display to generate synthetic binding proteins using a sweet protein, monellin, as a non-antibody scaffold. Single-chain monellin (scMonellin), in which two polypeptide chains of natural monellin are connected by a short linker, has two loops on one side of the molecule.

    Monellin - an overview | ScienceDirect Topics

    Monellin is a sweet protein that was isolated from the fruit of Dioscoreophyllum cumminsii (Stapf) Diels, which is known as the serendipity berry and is native to West Africa. It is a basic protein with an isoelectric point of approximately 9.3 and is 3000 times sweeter than sucrose. 65,66 Perception lasts for more than 1 h and leaves an ...