Dodger
Thu, Feb-24-05, 19:19
Below are selected portions of a paper by Ravi Kant which discusses using natually occuring sweet proteins to replace the artificial sweeteners that most of us use. The whole paper can be found at http://www.nutritionj.com/content/4/1/5
Abstract
Exponential growth in the number of patients suffering from diseases caused by the consumption of sugar has become a threat to mankind's health. Artificial low calorie sweeteners available in the market may have severe side effects. It takes time to figure out the long term side effects and by the time these are established, they are replaced by a new low calorie sweetener. Saccharine has been used for centuries to sweeten foods and beverages without calories or carbohydrate. It was also used on a large scale during the sugar shortage of the two world wars but was abandoned as soon as it was linked with development of bladder cancer. Naturally occurring sweet and taste modifying proteins are being seen as potential replacements for the currently available artificial low calorie sweeteners. Interaction aspects of sweet proteins and the human sweet taste receptor are being investigated.
Sweet and taste modifying proteins
The prevalence of obesity and diabetes has increased dramatically in recent years in the United States, with similar patterns seen in several other countries including India as well. Diabetes mellitus is a chronic disease caused by inherited or acquired deficiency in production of insulin by the pancreas or by the ineffectiveness of the insulin produced. Artificial sweeteners like Saccharin, Aspartame, Cyclamate and AcesulfameK are used world-wide as low calorie sweeteners by patients affected by diseases linked to the consumption of sugar, e.g. diabetes, hyperlipemia, caries, obesity etc. but they have side effects such as psychological problems, mental disorders, bladder cancer, heart failure and brain tumors. Sweet proteins have the potential to replace these artificial sweeteners, by acting as natural, good, low calorie sweeteners, as we know that proteins do not trigger a demand for insulin in these patients whereas sucrose does.
In humans, the sweet taste is mainly due to the recently discovered T1R2-T1R3 receptor, two of the three members of the T1R class of taste-specific proteins hypothesized to function in combination as a heterodimer. The human T1R2-T1R3 receptor recognizes natural and synthetic sweetness and T1R1-T1R3 recognizes umami taste. So far there are seven known sweet and taste-modifying proteins, namely Brazzein, Thaumatin, Monelin, Curculin, Mabinlin, Miraculin and Pentadin. The key residues on the protein surface responsible for biological activity have not yet been identified with certainty for any of these proteins. Monellin was found to be 100000 times sweeter than sucrose on a molar basis, followed by Brazzein and Thaumatin which are 500 times and 3000 times sweeter then sucrose respectively (the latter two on a weight basis). All of these proteins have been isolated from plants that grow in tropical rainforests. Although most of them share no sequence homology or structural similarity, Thaumatin shares extensive homology with certain non-sweet proteins found in other plants.
The potential industrial applications of these proteins are the low calorie sweetener industry and the cola, snacks, food and chocolate industries.
Conclusion and scope of further work
As it has been found that sweet proteins are thousands of times sweeter than sucrose and are of low calorie value, these proteins can be used as natural low calorie sweeteners by people suffering from diseases linked to consumption of sugar e.g. obesity, diabetes and hyperlipemia.
Candidate proteins can be checked for biological activity with the human taste receptor. Also mutations can be induced in candidate sweet proteins to analyze changes in their physical, chemical and biological properties. The work can be taken forward by solving the structures of the proteins and taste receptors with a view to increasing the efficiency of these sweeteners.
Abstract
Exponential growth in the number of patients suffering from diseases caused by the consumption of sugar has become a threat to mankind's health. Artificial low calorie sweeteners available in the market may have severe side effects. It takes time to figure out the long term side effects and by the time these are established, they are replaced by a new low calorie sweetener. Saccharine has been used for centuries to sweeten foods and beverages without calories or carbohydrate. It was also used on a large scale during the sugar shortage of the two world wars but was abandoned as soon as it was linked with development of bladder cancer. Naturally occurring sweet and taste modifying proteins are being seen as potential replacements for the currently available artificial low calorie sweeteners. Interaction aspects of sweet proteins and the human sweet taste receptor are being investigated.
Sweet and taste modifying proteins
The prevalence of obesity and diabetes has increased dramatically in recent years in the United States, with similar patterns seen in several other countries including India as well. Diabetes mellitus is a chronic disease caused by inherited or acquired deficiency in production of insulin by the pancreas or by the ineffectiveness of the insulin produced. Artificial sweeteners like Saccharin, Aspartame, Cyclamate and AcesulfameK are used world-wide as low calorie sweeteners by patients affected by diseases linked to the consumption of sugar, e.g. diabetes, hyperlipemia, caries, obesity etc. but they have side effects such as psychological problems, mental disorders, bladder cancer, heart failure and brain tumors. Sweet proteins have the potential to replace these artificial sweeteners, by acting as natural, good, low calorie sweeteners, as we know that proteins do not trigger a demand for insulin in these patients whereas sucrose does.
In humans, the sweet taste is mainly due to the recently discovered T1R2-T1R3 receptor, two of the three members of the T1R class of taste-specific proteins hypothesized to function in combination as a heterodimer. The human T1R2-T1R3 receptor recognizes natural and synthetic sweetness and T1R1-T1R3 recognizes umami taste. So far there are seven known sweet and taste-modifying proteins, namely Brazzein, Thaumatin, Monelin, Curculin, Mabinlin, Miraculin and Pentadin. The key residues on the protein surface responsible for biological activity have not yet been identified with certainty for any of these proteins. Monellin was found to be 100000 times sweeter than sucrose on a molar basis, followed by Brazzein and Thaumatin which are 500 times and 3000 times sweeter then sucrose respectively (the latter two on a weight basis). All of these proteins have been isolated from plants that grow in tropical rainforests. Although most of them share no sequence homology or structural similarity, Thaumatin shares extensive homology with certain non-sweet proteins found in other plants.
The potential industrial applications of these proteins are the low calorie sweetener industry and the cola, snacks, food and chocolate industries.
Conclusion and scope of further work
As it has been found that sweet proteins are thousands of times sweeter than sucrose and are of low calorie value, these proteins can be used as natural low calorie sweeteners by people suffering from diseases linked to consumption of sugar e.g. obesity, diabetes and hyperlipemia.
Candidate proteins can be checked for biological activity with the human taste receptor. Also mutations can be induced in candidate sweet proteins to analyze changes in their physical, chemical and biological properties. The work can be taken forward by solving the structures of the proteins and taste receptors with a view to increasing the efficiency of these sweeteners.