Recent developments in the characterization and biotechnological production of sweet-tasting proteins

Faus, Ignacio

doi:10.1007/s002530050001

Cited by 106 publications

(64 citation statements)

References 21 publications

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“…45 Thaumatin is intensely sweet (that is, 3000 times sweeter than sucrose) and is approved as a food-grade ingredient. Production by A. niger var.…”

Section: Prebioticsmentioning

confidence: 99%

Production of valuable compounds by molds and yeasts

Demain

Martens

2016

J Antibiot

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where he has contributed in a major way to the reputation of this department for many years. He also served as an Adjunct Professor at the University of Geneva. Among Julian's areas of study and accomplishment are fungal toxins including α-sarcin, chemical synthesis of triterpenes, mode of action of streptomycin and other aminoglycoside antibiotics, biochemical mechanisms of antibiotic resistance in clinical isolates of bacteria harboring resistance plasmids, their origins and evolution, secondary metabolism of microorganisms, structure and function of bacterial ribosomes, antibiotic resistance mutations in yeast ribosomes, cloning of resistance genes from an antibiotic-producing microbe, gene cloning for industrial purposes, engineering of herbicide resistance in useful crops, bleomycin-resistance gene in clinical isolates of Staphylococcus aureus and many other topics. He has been an excellent teacher, lecturing in both English and French around the world, and has organized international courses. Julian has also served on the NIH study sections, as Editor for several international journals, and was one of the founders of the journal Plasmid. We expect the impact of Julian's accomplishments to continue into the future.

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“…45 Thaumatin is intensely sweet (that is, 3000 times sweeter than sucrose) and is approved as a food-grade ingredient. Production by A. niger var.…”

Section: Prebioticsmentioning

confidence: 99%

Production of valuable compounds by molds and yeasts

Demain

Martens

2016

J Antibiot

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“…Six sweet tasting proteins, ranging in size from 6 to ϳ22 kDa, have been discovered (13). The mass of these protein sweeteners makes them too large to fit within the presumptive small molecule-binding pocket, suggesting that they stabilize the active conformation of the sweet receptor in a different manner.…”

mentioning

confidence: 99%

The Cysteine-rich Region of T1R3 Determines Responses to Intensely Sweet Proteins

Jiang¹,

et al. 2004

Journal of Biological Chemistry

262

225

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A wide variety of chemically diverse compounds taste sweet, including natural sugars such as glucose, fructose, sucrose, and sugar alcohols, small molecule artificial sweeteners such as saccharin and acesulfame K, and proteins such as monellin and thaumatin. Brazzein, like monellin and thaumatin, is a naturally occurring plant protein that humans, apes, and Old World monkeys perceive as tasting sweet but that is not perceived as sweet by other species including New World monkeys, mouse, and rat. It has been shown that heterologous expression of T1R2 plus T1R3 together yields a receptor responsive to many of the above-mentioned sweet tasting ligands. We have determined that the molecular basis for species-specific sensitivity to brazzein sweetness depends on a site within the cysteine-rich region of human T1R3. Other mutations in this region of T1R3 affected receptor activity toward monellin, and in some cases, overall efficacy to multiple sweet compounds, implicating this region as a previously unrecognized important determinant of sweet receptor function.Obesity and diabetes have reached epidemic proportions in developed societies. Although in part this is because of a more sedentary lifestyle, our strong preference for sweet tasting foods and their abundance is a major factor. Replacing sugar with low-or non-caloric sweeteners may be of benefit. To design more effective sweeteners it is important to understand at the molecular level how the sweet taste receptor functions. It has been demonstrated that the combination of T1R2 ϩ T1R3 recognizes and responds to many sweet ligands, including sugars, small molecule artificial sweeteners, and protein sweeteners (1, 2).T1R2 and T1R3 are subclass 3 G-protein-coupled receptors (1-7). Other members of this subclass are metabotropic glutamate receptors (mGluRs), 1 calcium-sensing receptors, pheromone receptors, and other taste/olfactory receptors (T1R1, 5.24 odor receptor) (8). Each member of this family has a large extracellular amino-terminal domain (ATD) followed by a cysteine-rich linker domain and a seven-transmembrane-spanning helical region.The solved crystal structures of the ATD of homodimeric metabotropic glutamate type 1 receptor (mGluR1) show that the mGluR1 ligand-binding region consists of two amino-terminal protomers (9). Each protomer comprises LB1 and LB2 domains that form a clamshell-like structure with the ligandbinding domain lying between LB1 and LB2. The free-form I (open-open_R) is thought to be in the resting state, whereas the free-form II (closed-open_A) is thought to be the active state. Agonist binding stabilizes the active closed-open_A conformer and promotes a shift of equilibrium toward the active state. The role of the cysteine-rich region, which links the ATD to the transmembrane domain, is presently unknown.Based on sequence homology and predicted secondary structural similarity to mGluR1, it seems likely that the T1R2 ϩ T1R3 sweet receptor will also have open-open and open-closed forms and that small sweet compounds may stabilize the ac...

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“…TLPs do not have a sweet taste 81 . TLPs from cold acclimated wheat grass is used to prevent the recrystallisation of water in frozen foods 173 .…”

Section: Thaumatin-like Proteins (Tlps) (Pr-5)mentioning

confidence: 99%

A Review: Biological and Technological Functions of Barley Seed Pathogenesis-Related Proteins (PRs)

Gorjanović

2009

Journal of the Institute of Brewing

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The mature barley seed proteome is dominated by proteins involved in stress responses, including the Pathogenesis-Related proteins (PRs). PRs are currently classified into 17 families. The biochemistry of the PRs families, whose members are constitutively present in barley seed, is surveyed in this paper. These proteins are assumed to protect dormant and germinating seeds against pathogenic microorganisms and pests. The current knowledge on PRs structural and functional properties is summarized in an attempt to illustrate their importance in barley seed innate resistance. At the same time, a platform to understand PRs technological function in cereal foods and in beverage processing and quality is provided.

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Recent developments in the characterization and biotechnological production of sweet-tasting proteins

Cited by 106 publications

References 21 publications

Production of valuable compounds by molds and yeasts

Production of valuable compounds by molds and yeasts

The Cysteine-rich Region of T1R3 Determines Responses to Intensely Sweet Proteins

A Review: Biological and Technological Functions of Barley Seed Pathogenesis-Related Proteins (PRs)

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