scholarly journals Conversion of amino acids to aryl/heteroaryl ethanol metabolites using human CYP2D6-expressing live baker's yeast

2020 ◽  
Vol 11 (1) ◽  
pp. 142-147
Author(s):  
Monika Bhardwaj ◽  
Shifali Chib ◽  
Loveleena Kaur ◽  
Amit Kumar ◽  
Bhabatosh Chaudhuri ◽  
...  
Keyword(s):  
Amino Acids ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Ethanol Metabolites

Biotransformation of amino acids into aryl/heteroaryl ethanol metabolites using human CYP2D6 for developing a potential anti-depressant agent.

scholarly journals Radiochemical determination of a unique sequence around the reactive serine residue of a di-isopropyl phosphorofluoridate-sensitive plant carboxypeptidase and a yeast peptidase

1972 ◽  
Vol 128 (2) ◽  
pp. 229-235 ◽  
Author(s):  
D. C. Shaw ◽  
J. R. E. Wells
Keyword(s):  
Amino Acids ◽  
French Bean ◽  
Unique Sequence ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Serine Carboxypeptidase ◽  
Serine Residue ◽  
Radiochemical Determination ◽  
Bean Leaves

Phaseolain, a carboxypeptidase from French-bean leaves, and a partially purified peptidase from baker's yeast are inhibited by reaction with di-isopropyl phosphorofluoridate. Radioactive di-isopropyl [32P]phosphorofluoridate was used to show that the site of reaction is a unique serine residue and that the sequence of amino acids adjacent to the reactive serine is Glu-Ser-Tyr. This sequence is different from those of other ‘serine’ enzymes previously reported and, for phaseolain, represents an unequivocal example of a ‘serine’ carboxypeptidase.

Use of Selected Sourdough Strains of Lactobacillus for Removing Gluten and Enhancing the Nutritional Properties of Gluten-Free Bread

2008 ◽  
Vol 71 (7) ◽  
pp. 1491-1495 ◽  
Author(s):  
RAFFAELLA DI CAGNO ◽  
CARLO G. RIZZELLO ◽  
MARIA DE ANGELIS ◽  
ANGELA CASSONE ◽  
GIAMMARIA GIULIANI ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Free Amino ◽  
Spectrophotometric Analysis ◽  
Baker’S Yeast ◽  
Phytase Activity ◽  
Baker's Yeast ◽  
Gluten Free ◽  
Nutritional Properties ◽  
Long Time

Forty-six strains of sourdough lactic acid bacteria were screened for proteolytic activity and acidification rate in gluten-free (GF) flours. The sourdough cultures consisted of Lactobacillus sanfranciscensis LS40 and LS41 and Lactobacillus plantarum CF1 and were selected and used for the manufacture of GF bread. Fermentation occurred in two steps: (i) long-time fermentation (16 h) and (ii) fast fermentation (1.5 h) using the previous fermented sourdough as inoculum (ca. 43%, wt/wt) with Saccharomyces cerevisiae (baker's yeast). GF bread started with baker's yeast alone was used as the control. Gluten was added to ingredients before fermentation to simulate contamination. Initial gluten concentration of 400 ppm was degraded to below 20 ppm only in the sourdough GF bread. Before baking, sourdough GF bread showed phytase activity ca. sixfold higher than that of GF bread started with baker's yeast alone. Atomic absorption spectrophotometric analysis revealed that the higher phytase activity resulted in an increased availability of free Ca2+, Zn2+, and Mg2+. The concentration of free amino acids also was the highest in sourdough GF bread. Sourdough GF bread had a higher specific volume and was less firm than GF bread started with baker's yeast alone. This study highlighted the use of selected sourdough cultures to eliminate risks of contamination by gluten and to enhance the nutritional properties of GF bread.

scholarly journals 2nSILAC for Quantitative of Prototrophic Baker’s Yeast

2021 ◽  
pp. 253-270
Author(s):  
Stefan Dannenmaier ◽  
Silke Oeljeklaus ◽  
Bettina Warscheid
Keyword(s):  
Amino Acids ◽  
Stable Isotope ◽  
Isotope Labeling ◽  
High Resolution Mass Spectrometry ◽  
Model Organism ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Genetic Manipulations ◽  
Genome Wide ◽  
Generic Strategy

AbstractStable isotope labeling by amino acids in cell culture (SILAC) combined with high-resolution mass spectrometry is a quantitative strategy for the comparative analysis of (sub)proteomes. It is based on the metabolicincorporation of stable isotope-coded amino acids during growth of cells or organisms. Here, complete labeling of proteins with the amino acid(s) selected for incorporation needs to be guaranteed to enable accurate quantification on a proteomic scale. Wild-type strains of baker’s yeast (Saccharomyces cerevisiae), which is a widely accepted and well-studied eukaryotic model organism, are generally able to synthesize all amino acids on their own (i.e., prototrophic). To render them amenable to SILAC, auxotrophies are introduced by genetic manipulations. We addressed this limitation by developing a generic strategy for complete “native” labeling of prototrophic S. cerevisiae with isotope-coded arginine and lysine, referred to as “2nSILAC”. It allows for directly using and screening several genome-wide yeast mutant collections that are easily accessible to the scientific community for functional proteomic studies but are based on prototrophic variants of S. cerevisiae.

Biosynthesis of Branched-Chain Amino Acids in Schizosaccharomyces pombe: Regulation of the Enzymes Involved in Isoleucine, Valine, and Leucine Synthesis

1974 ◽  
Vol 52 (1) ◽  
pp. 51-59 ◽  
Author(s):  
Roderick A. McDonald ◽  
T. Satyanarayana ◽  
J. G. Kaplan
Keyword(s):  
Amino Acids ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Feedback Inhibition ◽  
Branched Chain Amino Acids ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Threonine Deaminase ◽  
Branched Chain ◽  
Ph Range

The activities and regulation of the enzymes of the synthetic pathway of branched-chain amino acids were investigated in the fission yeast, Schizosaccharomyces pombe. Previous studies had shown the presence of threonine deaminase (TD) and acetohydroxy acid synthetase (AHAS). The remaining isoleucine–valine enzymes, isomeroreductase (IR), dehydrase, and transaminase B, have now been characterized in cell-free extracts, indicating the presence in this yeast of the complete pathway as demonstrated in other microorganisms. α-Isopropylmalate synthetase (IPMS), the first enzyme of the leucine pathway, has properties of a typical regulatory enzyme; it is most active in the pH range 7.5–8.5, but is most sensitive to feedback inhibition by L-leucine at pH 6.5–7.0. Unlike the situation in baker's yeast, only AHAS and IR appeared to be subject to multivalent repression. TD was relatively resistant to any change in level, and AHAS was repressible by valine included in the growth medium. IPMS was repressed when cells were grown in complex medium; leucine alone did not cause repression, and in contrast with baker's yeast, neither did leucine plus threonine or a combination of all three branched-chain amino acids.

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