scholarly journals A continuous fermentation technique for studying the kinetics of sugar uptake by baker's yeast

1966 ◽  
Vol 100 (2) ◽  
pp. 556-563 ◽  
Author(s):  
WE Trevelyan
Fermentation ◽  
2019 ◽  
Vol 6 (1) ◽  
pp. 2 ◽  
Author(s):  
Antonio Alfonzo ◽  
Raimondo Gaglio ◽  
Marcella Barbera ◽  
Nicola Francesca ◽  
Giancarlo Moschetti ◽  
...  

The present work was carried out to evaluate the microbiological, physicochemical, and sensory characteristics of fortified pistachio breads. Pistachio powder (5% w/w) was added to flour or semolina and fermented by a commercial baker’s yeast (Saccharomyces cerevisiae). Pistachio powder did not influence the biological leavening of the doughs. The kinetics of pH and total titratable acidity (TTA) during dough fermentation showed that the leavening process occurred similarly for all trials. The concentration of yeasts increased during fermentation and reached levels of 108 CFU/g after 2 h. Pistachio powder decreased the height and softness of the final breads and increased cell density of the central slices. The amount of lysine after baking increased in pistachio breads and this effect was stronger for semolina rather than flour trials. Sensory evaluation indicated that fortified breads processed from semolina were those more appreciated by the judges. This work clearly indicated that the addition of pistachio powder in bread production represents a promising strategy to increase the availability of lysine in cereal-based fermented products.


2007 ◽  
Vol 39 (2) ◽  
pp. 85-91 ◽  
Author(s):  
Don-Hee Park ◽  
George W. Malaney ◽  
Robert D. Tanner

2003 ◽  
Vol 89 (3) ◽  
pp. 281-287 ◽  
Author(s):  
Padma Vasudevan ◽  
V Padmavathy ◽  
S.C Dhingra

1992 ◽  
Vol 8 (1-2) ◽  
pp. 39-47 ◽  
Author(s):  
W. J. Groot ◽  
C. M. Sikkenk ◽  
R. H. Waldram ◽  
R. G. J. M. Lans ◽  
K. Ch. A. M. Luyben

1976 ◽  
Vol 157 (2) ◽  
pp. 389-393 ◽  
Author(s):  
B J Gould ◽  
M A Goheer

1. The reaction catalysed by glucose 6-phosphate dehydrogenase (D-glucose 6-phosphate-NADP+ oxidoreductase, EC 1.1.1.49) from baker's yeast was studied in 42mM-glycylglycine buffer, pH7.4 at 25 degrees C, by initial-velocity studies and by the use of NADPH as a product inhibitor. 2. The reactions catalysed by both the soluble enzyme and a stable enzyme covalently attached to CNBr-activated Sepharose 4B probably follow an ordered reaction mechanism with NADP+ and NADPH as the leading reactants. 3. The kinetic constants obtained for the soluble enzyme lere: KNADP+m, 19 muM; KNADP+s, 23 muM; KNADPHs, 15 muM. Similar values were obtained for the immobilized enzyme. 4. The assay of the immobilized enzyme was done by using a micro packed-bed recirculation reactor, and the advantages of this technique are discussed.


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