Comparative Studies on the Dodecameric and Hexameric Forms of Yeast Aminopeptidase I

1979 ◽  
Vol 34 (5-6) ◽  
pp. 381-386 ◽  
Author(s):  
H.-G. Löffler ◽  
K.-H. Rohm

Abstract Yeast Aminopeptidase I, Molecular Forms, Immunological Behaviour Yeast aminopeptidase I, when purified from autolysates of brewer’s yeast, is obtained in two molecular forms a) the enzymatically active dodecameric complex (Mr = 640 000, s20, w = 22 S) and b) inactive hexamers (Mr = 320 000, s20, w = 12 S). Although the amino acid composition of the 12 S protein is very similar to that of the active enzyme, the hexamers behave differently in ionic exchange chromatography and during electrophoresis on polyacrylamide gels. Moreover, the antigenic properties of 12 S and 22 S aminopeptidase forms suggest a considerable degree of structural diversity. Several strains of Saccharomyces cerevisiae did not contain hexameric forms although their 22 S aminopeptidase was immunologically indistinguishable from brewer’s yeast amino­ peptidase. It is proposed that the hexameric protein is the result of “unproductive ” aggregation of aminopeptidase subunits.

Materials ◽  
2020 ◽  
Vol 13 (16) ◽  
pp. 3624 ◽  
Author(s):  
Inga Zinicovscaia ◽  
Nikita Yushin ◽  
Daler Abdusamadzoda ◽  
Dmitrii Grozdov ◽  
Margarita Shvetsova

The performance of the brewer’s yeast Saccharomyces cerevisiae to remove metal ions from four batch systems, namely Zn(II), Zn(II)-Sr(II)-Cu(II), Zn(II)-Ni(II)-Cu(II), and Zn(II)-Sr(II)-Cu(II)-Ba(II), and one real effluent was evaluated. Yeast biosorption capacity under different pH, temperature, initial zinc concentration, and contact time was investigated. The optimal pH for removal of metal ions present in the analyzed solution (Zn, Cu, Ni, Sr, and Ba) varied from 3.0 to 6.0. The biosorption process for zinc ions in all systems obeys Langmuir adsorption isotherm, and, in some cases, the Freundlich model was applicable as well. The kinetics of metal ions biosorption was described by pseudo-first-order, pseudo-second-order, and Elovich models. Thermodynamic calculations showed that metal biosorption was a spontaneous process. The two-stage sequential scheme of zinc ions removal from real effluent by the addition of different dosages of new sorbent allowed us to achieve a high efficiency of Zn(II) ions removal from the effluent. FTIR revealed that OH, C=C, C=O, C–H, C–N, and NH groups were the main biosorption sites for metal ions.


2011 ◽  
Vol 198 (12) ◽  
pp. 1594-1602 ◽  
Author(s):  
Phungjai Boonyeun ◽  
Artiwan Shotipruk ◽  
Chattip Prommuak ◽  
Manop Suphantharika ◽  
Chirakarn Muangnapoh

2018 ◽  
Vol 54 (2C) ◽  
pp. 458
Author(s):  
Nguyen Thi Thanh Ngoc

Brewer’s yeast spent, obtained after the main fermentation stage, is a rich- in-protein source(protein content accounts for 48 - 50 % dry matter). In order to use efficiently this source, it washydrolysed by different methods. Protein hydrolysate products are normally mixtures of peptidesand amino acids. Protein hydrolysates have a wide range of applications in food. It can be usedas emulsifying agents in a number of applications such as salad dressings, spreads, ice cream,coffee whitener, cracker, and meat products like sausages. However, bitterness in hydrolysates isone of the major undesirable aspects for various applications in food processing. In this study,we used enzymatic mixture alcalase and flavourzyme, yeast treatment methods to hydrolysebrewer’s yeast. The hydrolysate and fractions of protein hydrolysate obtained after filtration with10 kDa and 3 kDa filters were used for determination of bitterness and hydrophobic amino acidscontent. The bitter taste of hydrolysate was determined by sensory method (using quininestandard) and amino acid content was analysed by HPLC method. The result showed the closerelationship between bitter taste and hydrophobic amino acid content. The bitter taste of proteinhydrolysate was reduced as the hydrophobic amino acid content decreased. When the bitter taste(equivalent to quinine concentration) decreased from 16.25 μmol/l to 3.59 μmol/l, the totalcontent of hydrophobic amino acids in protein hydrolysate reduced from 1653 μg/ml to 932μg/ml.


2019 ◽  
Vol 45 (6) ◽  
pp. 1801-1812 ◽  
Author(s):  
Bruno Olivetti de Mattos ◽  
José Fernando López-Olmeda ◽  
Bartira Guerra-Santos ◽  
Cristóbal Espinosa Ruiz ◽  
José María García-Beltrán ◽  
...  

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