Modification of yeast characteristics by soy peptides: cultivation with soy peptides represses the formation of lipid bodies

Ikeda, Kayo; Kitagawa, Sayuri; Tada, Takakiyo; Iefuji, Haruyuki; Inoue, Yoshiharu; Izawa, Shingo

doi:10.1007/s00253-010-3001-9

Cited by 16 publications

(7 citation statements)

References 28 publications

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“…Moreover, hydrolyzed casein (and not the intact protein) was found to possess hypolipidemic activities in obese-prone male C57BL/6J mice [16]. Furthermore, soy peptides decreased TG accumulation in yeast through the downregulation of lipogenic DGA1 mRNA compared to treatments with proteins or amino acid mixture of similar amino acid composition [17]. These findings support the direct hypolipidemic effects of food protein-derived peptides.…”

Section: Dietary Peptides and Hyperlipidemiamentioning

confidence: 89%

The Role of Food Peptides in Lipid Metabolism during Dyslipidemia and Associated Health Conditions

Udenigwe

Rouvinen‐Watt

2015

IJMS

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Animal and human clinical studies have demonstrated the ability of dietary food proteins to modulate endogenous lipid levels during abnormal lipid metabolism (dyslipidemia). Considering the susceptibility of proteins to gastric proteolytic activities, the hypolipidemic functions of proteins are possibly due, in part, to their peptide fragments. Food-derived peptides may directly modulate abnormal lipid metabolism in cell cultures and animal models of dyslipidemia. The peptides are thought to act by perturbing intestinal absorption of dietary cholesterol and enterohepatic bile acid circulation, and by inhibiting lipogenic enzymatic activities and gene expression in hepatocytes and adipocytes. Recent evidence indicates that the hypolipidemic activities of some peptides are due to activation of hepatic lipogenic transcription factors. However, detailed molecular mechanisms and structural requirements of peptides for these activities are yet to be elucidated. As hypolipidemic peptides can be released during enzymatic food processing, future studies can explore the prospects of combating metabolic syndrome and associated complications using peptide-rich functional food and nutraceutical products.

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Section: Dietary Peptides and Hyperlipidemiamentioning

confidence: 89%

The Role of Food Peptides in Lipid Metabolism during Dyslipidemia and Associated Health Conditions

Udenigwe

Rouvinen‐Watt

2015

IJMS

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“…Moreover, various physiological functions of soy peptides on microorganism cells have also been reported. Cultivation of yeast cells in medium containing soy peptides could improve the tolerance to freeze–thaw stress of baker's yeast, repress the formation of lipid bodies and accelerate alcoholic fermentation of brewer's yeast (Izawa et al ., ; Kitagawa et al ., ; Ikeda et al ., ). All these findings indicated that soy peptides can modify the characteristics of brewer's yeast.…”

Section: Introductionmentioning

confidence: 97%

Effects of soy protein hydrolysates on the growth and fermentation performances of brewer's yeast

Zhao

Wan

Zhao

et al. 2014

Int J of Food Sci Tech

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Soy protein isolate was hydrolysed with Alcalase, Papain, Flavorzyme and Protemax, respectively, and further fractioned by ultrafiltration. The resulting soy protein hydrolysates (SPH) and their ultrafiltration fractions were used to examine their effects on the growth and fermentation performances of brewer's yeast. Results showed that degree of hydrolysis, molecular weight distribution and amino acid composition of SPH significantly affected the growth, viability and fermentation performance of brewer's yeast. The SPH prepared from different proteolytic enzymes exhibited distinct growth-and fermentation-promoting activity for brewer's yeast. The SPH treated with Protemax for 9 h and with the molecular weight below 3 kDa showed the highest growth-promoting activity and induced more rapidly reducing sugar consumption and higher ethanol production. The relatively lower molecular weight and the hydrophilic and electropositive amino acid residues (Lys, His, Arg and Ile) in SPH might be responsible for its functionality, promoting the growth and fermentation of brewer's yeast.

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“…For example, soy peptides, the proteolytic products of soy proteins, can reduce serum lipid levels, scavenge free radicals, and reduce oxidative stress in mammalian cells (6)(7)(8). In yeast, soy peptides improve tolerance to freeze-thaw stress, repress the formation of lipid bodies (9), and accelerate ethanol fermentation (10,11). hPepT1 and hPepT2 are human peptide transporters expressed in the small intestine and the kidney, respectively (12).…”

mentioning

confidence: 99%

Functional Implications and Ubiquitin-Dependent Degradation of the Peptide Transporter Ptr2 in Saccharomyces cerevisiae

et al. 2014

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The peptide transporter Ptr2 plays a central role in di-or tripeptide import in Saccharomyces cerevisiae. Although PTR2 transcription has been extensively analyzed in terms of upregulation by the Ubr1-Cup9 circuit, the structural and functional information for this transporter is limited. Here we identified 14 amino acid residues required for peptide import through Ptr2 based on the crystallographic information of Streptococcus thermophilus peptide transporter PepT st and based on the conservation of primary sequences among the proton-dependent oligopeptide transporters (POTs). Expression of Ptr2 carrying one of the 14 mutations of which the corresponding residues of PepT st are involved in peptide recognition, salt bridge interaction, or peptide translocation failed to enable ptr2⌬trp1 cell growth in alanyl-tryptophan (Ala-Trp) medium. We observed that Ptr2 underwent rapid degradation after cycloheximide treatment (half-life, approximately 1 h), and this degradation depended on Rsp5 ubiquitin ligase. The ubiquitination of Ptr2 most likely occurs at the N-terminal lysines 16, 27, and 34. Simultaneous substitution of arginine for the three lysines fully prevented Ptr2 degradation. Ptr2 mutants of the presumed peptide-binding site (E92Q, R93K, K205R, W362L, and E480D) exhibited severe defects in peptide import and were subjected to Rsp5-dependent degradation when cells were moved to Ala-Trp medium, whereas, similar to what occurs in the wild-type Ptr2, mutant proteins of the intracellular gate were upregulated. These results suggest that Ptr2 undergoes quality control and the defects in peptide binding and the concomitant conformational change render Ptr2 subject to efficient ubiquitination and subsequent degradation.

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Modification of yeast characteristics by soy peptides: cultivation with soy peptides represses the formation of lipid bodies

Cited by 16 publications

References 28 publications

The Role of Food Peptides in Lipid Metabolism during Dyslipidemia and Associated Health Conditions

The Role of Food Peptides in Lipid Metabolism during Dyslipidemia and Associated Health Conditions

Effects of soy protein hydrolysates on the growth and fermentation performances of brewer's yeast

Functional Implications and Ubiquitin-Dependent Degradation of the Peptide Transporter Ptr2 in Saccharomyces cerevisiae

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