2015
DOI: 10.1016/j.foodchem.2014.10.151
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Design of sweet protein based sweeteners: Hints from structure–function relationships

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Cited by 40 publications
(36 citation statements)
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References 38 publications
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“…This protein and its derivatives have been proposed as potential low‐calorie sugar replacers for food and beverages, but their usage in this framework has been slowed down by their intrinsic structural fragility. Although displaying higher thermal stability than the heterodimeric natural precursor monellin , MNEI is still sensitive to combinations of pH and temperature values, that can trigger its unfolding, aggregation and precipitation, with consequent loss of activity . In recent years, MNEI has also become a well‐accepted model to study folding and aggregation properties of β‐sheet‐rich proteins.…”
Section: Discussionmentioning
confidence: 99%
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“…This protein and its derivatives have been proposed as potential low‐calorie sugar replacers for food and beverages, but their usage in this framework has been slowed down by their intrinsic structural fragility. Although displaying higher thermal stability than the heterodimeric natural precursor monellin , MNEI is still sensitive to combinations of pH and temperature values, that can trigger its unfolding, aggregation and precipitation, with consequent loss of activity . In recent years, MNEI has also become a well‐accepted model to study folding and aggregation properties of β‐sheet‐rich proteins.…”
Section: Discussionmentioning
confidence: 99%
“…One of the factors that strongly affects the outcome of such a process is pH. In fact, monellin stability is pH‐dependent, and a shift from acidic to neutral or alkaline pH can significantly affect stability and physical properties . Studies on MNEI have recently demonstrated that changes of the external pH in the range 4.0–8.0 reflect on the protonation state of a single residue, Glu23, located in a buried pocket of the protein and possessing an unusually high p K a value .…”
mentioning
confidence: 99%
“…Among sweet substances, sweet proteins are receiving an increasing interest as low‐calorie sweeteners potentially appealing for food manufacturers and beneficial to those who need to control sugar intake, such as obese or diabetic people (Rega et al, ). The three best studied sweet proteins are monellin, brazzein, and thaumatin: their structure has been well characterized, and hypotheses about their mechanism of action have been formulated (Picone & Temussi, ; Temussi, ).…”
Section: Introductionmentioning
confidence: 99%
“…Recently, we have performed several studies (Di Monaco et al, ; Di Monaco, Miele, Volpe, Picone, & Cavella, ; Rega et al, ) to characterize the sweetness perception of MNEI protein and to compare it with commercial sweeteners, focusing on MNEI sweetness in liquid matrix. However, since both sweeteners and hydrocolloids are largely used ingredients in food industry, contributing to both functional and sensory properties, it is necessary to extend these studies to semisolid or solid media.…”
Section: Introductionmentioning
confidence: 99%
“…Despite artificial sweeteners (aspartame, saccharin, neotame, sucralose, and acesulfame potassium) have higher sweetness and lower calorie compared to sugar (Schiffman, 2012), yet these compounds are often linked to some diseases due to their side effects, including psychological problems, mental disorder, bladder cancer and heart failure (Masuda and Kitabatake, 2006). Some proteins have been known to elicit the sensation of sweetness (Gnanavel and Muthukumar, 2011;Rega et al, 2015;Masuda and Kitabatake, 2006). These proteins, so-called sweet tasting proteins, include thaumatin, monellin, mabinlin, brazzein, egg lysozyme, and neoculin (previously considered as curculin) (Picone and Temussi, 2012) are considered to be promising as low calorie sweeteners for sugar replacement (Masuda and Kitabatake, 2006).…”
Section: Introductionmentioning
confidence: 99%