scholarly journals EVALUATION OF ANTIOXIDANT JUICE CASHEW (Anacardium occidentale Linn) IN Saccharomyces cerevisiae BEFORE AND AFTER DRYING SPRAY

2013 ◽  
Vol 10 (19) ◽  
pp. 57-64
Author(s):  
Débora Cássia Vieira GOMES ◽  
Dayane Alves COSTA ◽  
Everton José Ferreira de ARAÚJO ◽  
Paula do Nascimento BATISTA ◽  
Márcio dos Santos ROCHA ◽  
...  

Compounds classified as antioxidants act by inhibiting or reducing the effects caused by free radicals. Several methods have been developed to obtain an evaluation, it is qualitative or quantitative, the antioxidant capacity of various compounds, both by chemical tests or by using biological tests. In this context, this study aimed to evaluate the stability of the antioxidant potential of the juice and the dry material of cashew ((Anacardium ocidentale Linn) before and after spray-drying technique in yeast Saccharomyces cerevisiae proficient and deficient in antioxidant defenses. The juice of A. occidentale L reduced the growth inhibition in all strains of tested, demonstrating its antioxidant potential. Among all four strains of yeast, the variants SOD2Δ WT and SOD showed higher percentages of reduction in growth inhibition before and after drying. Since the mutants SOD1Δ/SOD2Δ and SOD1Δ the substance tested had low antioxidant activity. The juice of pseudofruit of A. occidentale L showed antioxidant potential by increasing the survival of yeast, verified in the reduction of damage caused by hydrogen peroxide, before and after spray drying, which shows that the technique of spray drying did not alter the antioxidant potential of the material analyzed.

2021 ◽  
Author(s):  
Fernanda Thaís Vieira Rubio ◽  
CWI Haminiuk ◽  
Mayara Martins dos Santos ◽  
Marcelo Thomazini ◽  
Izabel Freitas Moraes ◽  
...  

Although Saccharomyces cerevisiae has shown potential utilization as a bio-vehicle for encapsulation, there are no reports about the functionality of natural colorants encapsulated using yeast cells. The main objectives of...


1988 ◽  
Vol 8 (4) ◽  
pp. 1591-1601
Author(s):  
S B Baim ◽  
F Sherman

The mRNA sequence and structures that modify and are required for translation of iso-1-cytochrome c in the yeast Saccharomyces cerevisiae were investigated with sets of CYC1 alleles having alterations in the 5' leader region. Measurements of levels of CYC1 mRNA and iso-1-cytochrome c in strains having single copies of altered alleles with nested deletions led to the conclusion that there is no specific sequence adjacent to the AUG initiator codon required for efficient translation. However, the nucleotides preceding the AUG initiator codon at positions -1 and -3 slightly modified the efficiency of translation to an order of preference similar to that found in higher cells. In contrast to large effects observed in higher eucaryotes, the magnitude of this AUG context effect in S. cerevisiae was only two- to threefold. Furthermore, introduction of hairpin structures in the vicinity of the AUG initiator codon inhibited translation, with the degree of inhibition related to the stability and proximity of the hairpin. These results with S. cerevisiae and published findings on other organisms suggest that translation in S. cerevisiae is more sensitive to secondary structures than is translation in higher eucaryotes.


2017 ◽  
Vol 35 (8) ◽  
pp. 1029-1042 ◽  
Author(s):  
A. Chandralekha ◽  
Anupama Rani ◽  
Hrishikesh A. Tavanandi ◽  
N. Amrutha ◽  
Umesh Hebbar ◽  
...  

1994 ◽  
Vol 5 (3) ◽  
pp. 283-296 ◽  
Author(s):  
M Florio ◽  
L K Wilson ◽  
J B Trager ◽  
J Thorner ◽  
G S Martin

Expression of pp60v-src, the transforming protein of Rous sarcoma virus, arrests the growth of the yeast Saccharomyces cerevisiae. To determine the basis of this growth arrest, yeast strains were constructed that expressed either wild-type v-src or various mutant v-src genes under the control of the galactose-inducible, glucose repressible GAL1 promoter. When shifted to galactose medium, cells expressing wild-type v-src ceased growth immediately and lost viability, whereas cells expressing a catalytically inactive mutant (K295M) continued to grow normally, indicating that the kinase activity of pp60v-src is required for its growth inhibitory effect. Mutants of v-src altered in the SH2/SH3 domain (XD4, XD6, SPX1, and SHX13) and a mutant lacking a functional N-terminal myristoylation signal (MM4) caused only a partial inhibition of growth, indicating that complete growth inhibition requires either targeting of the active kinase or binding of the kinase to phosphorylated substrates, or both. Cells arrested by v-src expression displayed aberrant microtubule structures, alterations in DNA content and elevated p34CDC28 kinase activity. Immunoblotting with antiphosphotyrosine antibody showed that many yeast proteins, including the p34CDC28 kinase, became phosphorylated at tyrosine in cells expressing v-src. Both the growth inhibition and the tyrosine-specific protein phosphorylation observed following v-src expression were reversed by co-expression of a mammalian phosphotyrosine-specific phosphoprotein phosphatase (PTP1B). However a v-src mutant with a small insertion in the catalytic domain (SRX5) had the same lethal effect as wild-type v-src, yet induced only very low levels of protein-tyrosine phosphorylation. These results indicate that inappropriate phosphorylation at tyrosine is the primary cause of the lethal effect of pp60v-src expression but suggest that only a limited subset of the phosphorylated proteins are involved in this effect.


1988 ◽  
Vol 8 (4) ◽  
pp. 1591-1601 ◽  
Author(s):  
S B Baim ◽  
F Sherman

The mRNA sequence and structures that modify and are required for translation of iso-1-cytochrome c in the yeast Saccharomyces cerevisiae were investigated with sets of CYC1 alleles having alterations in the 5' leader region. Measurements of levels of CYC1 mRNA and iso-1-cytochrome c in strains having single copies of altered alleles with nested deletions led to the conclusion that there is no specific sequence adjacent to the AUG initiator codon required for efficient translation. However, the nucleotides preceding the AUG initiator codon at positions -1 and -3 slightly modified the efficiency of translation to an order of preference similar to that found in higher cells. In contrast to large effects observed in higher eucaryotes, the magnitude of this AUG context effect in S. cerevisiae was only two- to threefold. Furthermore, introduction of hairpin structures in the vicinity of the AUG initiator codon inhibited translation, with the degree of inhibition related to the stability and proximity of the hairpin. These results with S. cerevisiae and published findings on other organisms suggest that translation in S. cerevisiae is more sensitive to secondary structures than is translation in higher eucaryotes.


2016 ◽  
Vol 76 (2) ◽  
pp. 539-544 ◽  
Author(s):  
A. C. Piovezan-Borges ◽  
C. Valério-Júnior ◽  
I. L. Gonçalves ◽  
A. A. Mielniczki-Pereira ◽  
A. T. Valduga

Abstract Yerba-mate (Ilex paraguariensis St. Hil) is mainly consumed as “chimarrão”, a hot drink highly appreciated in Brazil, Argentina, Paraguay and Uruguay. This study evaluated the antioxidant potential of aqueous extracts of I. paraguariensis precipitated with ethanol. The leaves were processed as for tea product (TM) and oxidized (OX). The antioxidant potential was evaluated in cells of Saccharomyces cerevisiae deficient in antioxidant defense genes. Three strains evaluated were: a wild (EG) and two mutants (ctt1Δ e ctt1Δsod1Δ). These strains were pre-treated with the yerba-mate extracts (TM e OX) and submitted to oxidative stress induced by hydrogen peroxide. None of the extracts produced loss of cell viability. The extracts exerted antioxidant activity, protecting the strains (except sod1∆ctt1∆). The TM extract was more effective than OX. I. paraguariensis extracts showed a potential to be explored in the development of new products.


2003 ◽  
Vol 370 (3) ◽  
pp. 785-792 ◽  
Author(s):  
Hugo NÁJERA ◽  
Miguel COSTAS ◽  
D. Alejandro FERNÁNDEZ-VELASCO

The reasons underlying the oligomeric nature of some proteins such as triosephosphate isomerase (TIM) are unclear. It has been proposed that this enzyme is an oligomer, mainly because of its stability rather than for functional reasons. To address this issue, the reversible denaturation and renaturation of the homodimeric TIM from baker's yeast (Saccharomyces cerevisiae) induced by guanidinium chloride and urea have been characterized by spectroscopic, functional and hydrodynamic techniques. The unfolding and refolding of this enzyme are not coincident after ‘conventional’ equilibrium times. Unfolding experiments did not reach equilibrium, owing to a very slow dissociation and/or unfolding process. By contrast, equilibrium was reached in the refolding direction. The simplest equilibrium pathway compatible with the obtained data was found to be a three-state process involving an inactive and expanded monomer. The Gibbs energy changes for monomer folding (ΔGfold0 = −16.6±0.7kJ·mol-1) and monomer association (ΔGassoc0 = −70.3±1.1kJ·mol-1) were calculated from data obtained in the two denaturants. From an analysis of the present data and data from the literature on the stability of TIM from different species and for other β/α barrels, and model simulations on the effect of stability in the catalytic activity of the enzyme, it is concluded that the low stability of the monomers is neither the only, nor the main, cause for the dimeric nature of TIM. There is interplay between function and stability.


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