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Life
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Structure, Function and New Developments of Sweet Proteins
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Structure, Function and New Developments of Sweet Proteins

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Synthetic Biology and Systems Biology".

Deadline for manuscript submissions: closed (18 December 2020) | Viewed by 8928

Special Issue Editors

Dr. Serena Leone

E-Mail Website
Guest Editor
Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy
Interests: Protein Chemistry; Structural Biology; Protein modelling; Protein Design
Prof. Dr. Delia Picone

E-Mail Website
Guest Editor
Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy
Interests: protein production; protein design, structure and interaction; biomolecular NMR; sweet proteins; protein stability

Special Issue Information

Dear Colleagues,

The focus on sugar reduction is nowadays stronger than ever because of the increasing impact and interplay of pathologies like diabetes, obesity and cardiovascular diseases, that spread to the point of becoming global epidemies. Governments and institutions worldwide have launched initiatives aimed at inverting these trends, promoting the adoption of healthy lifestyles and the introduction in the diet of new sweeteners. Following this lead, food industries are actively seeking new ways to replace sugar.

Sweet proteins, first discovered in the 70s in a few tropical plants, with their sweetness up to five orders of magnitude greater than sucrose, stand out as ideal candidates for the job, but several problems still need to be addressed before they can find application in real food and beverage preparations.

This Special Issue has the goal to present the latest developments in the field of sweet proteins studies, which cover multiple research areas, from the rational design of new variants to withstand the environment of industrial processes, to the structural and computational studies to elucidate their action and the interaction with the sweet taste receptor; from the development of new biotechnological tools for the production to the development of pilot food formulates and the study of their physiological effects. We will welcome original research article and reviews on each of these subjects. This way, we hope to present the readers with a multifaceted picture, in which theoretical studies on the mechanism of sweet taste perception meet applicative and industrial research, defining a multidisciplinary landscape which attracts an increasing number of researchers.

Dr. Serena Leone
Prof. Dr. Delia Picone
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Life is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • sweet proteins
  • protein design
  • sweet taste receptors
  • molecular modeling
  • protein/receptor interactions
  • protein biotechnological production
  • sugar reduction
  • tasting proteins

Published Papers (2 papers)

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Research

13 pages, 3713 KiB  
Article
A Super Stable Mutant of the Plant Protein Monellin Endowed with Enhanced Sweetness
by Masoud Delfi, Alessandro Emendato, Serena Leone, Eros Antonio Lampitella, Piero Porcaro, Gaetano Cardinale, Luigi Petraccone and Delia Picone
Life 2021, 11(3), 236; https://doi.org/10.3390/life11030236 - 12 Mar 2021
Cited by 9 | Viewed by 3093
Abstract
Sweet proteins are a class of proteins with the ability to elicit a sweet sensation in humans upon interaction with sweet taste receptor T1R2/T1R3. Single-chain Monellin, MNEI, is among the sweetest proteins known and it could replace sugar in many food and beverage [...] Read more.
Sweet proteins are a class of proteins with the ability to elicit a sweet sensation in humans upon interaction with sweet taste receptor T1R2/T1R3. Single-chain Monellin, MNEI, is among the sweetest proteins known and it could replace sugar in many food and beverage recipes. Nonetheless, its use is limited by low stability and high aggregation propensity at neutral pH. To solve this inconvenience, we designed a new construct of MNEI, dubbed Mut9, which led to gains in both sweetness and stability. Mut9 showed an extraordinary stability in acidic and neutral environments, where we observed a melting temperature over 20 °C higher than that of MNEI. In addition, Mut9 resulted twice as sweet than MNEI. Both proteins were extensively characterized by biophysical and sensory analyses. Notably, Mut9 preserved its structure and function even after 10 min boiling, with the greatest differences being observed at pH 6.8, where it remained folded and sweet, whereas MNEI lost its structure and function. Finally, we performed a 6-month shelf-life assessment, and the data confirmed the greater stability of the new construct in a wide range of conditions. These data prove that Mut9 has an even greater potential for food and beverage applications than MNEI. Full article
(This article belongs to the Special Issue Structure, Function and New Developments of Sweet Proteins)
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12 pages, 3275 KiB  
Article
Comparison of Different Signal Peptides for the Efficient Secretion of the Sweet-Tasting Plant Protein Brazzein in Pichia pastoris
by Fabrice Neiers, Christine Belloir, Nicolas Poirier, Christian Naumer, Michael Krohn and Loïc Briand
Life 2021, 11(1), 46; https://doi.org/10.3390/life11010046 - 13 Jan 2021
Cited by 18 | Viewed by 4950
Abstract
Brazzein is a small sweet-tasting protein found in the red berries of a West African evergreen shrub, Pentadiplandra brazzeana Baillon. Brazzein is highly soluble and stable over a large pH range and at high temperatures, which are characteristics that suggest its use as [...] Read more.
Brazzein is a small sweet-tasting protein found in the red berries of a West African evergreen shrub, Pentadiplandra brazzeana Baillon. Brazzein is highly soluble and stable over a large pH range and at high temperatures, which are characteristics that suggest its use as a natural sweetener. However, Pentadiplandra brazzeana culture is difficult at a large scale, limiting the natural source of brazzein. Heterologous expression of brazzein has been established in numerous systems, including bacteria, yeast, and transgenic plants. Brazzein requires four disulfide bonds to be active in eliciting an intense sweet taste, and the yeast Pichia pastoris appears to be one of the best options for obtaining functional brazzein in high quantities. Employing yeast secretion in the culture medium allows us to obtain fully active brazzein and facilitate purification later. To increase yeast secretion, we compared seven different signal peptides to successfully achieve brazzein secretion using the yeast P. pastoris. The brazzein proteins corresponding to these signal peptides elicited activation of the sweet taste receptor functionally expressed in a cellular assay. Among these tested signal peptides, three resulted in the secretion of brazzein at high levels. Full article
(This article belongs to the Special Issue Structure, Function and New Developments of Sweet Proteins)
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