Accumulation of Free L-Glutamic Acid in Full- and Reduced-fat Cheddar Cheese Ripened at Different Time/temperature Conditions

LWT ◽  
2001 ◽  
Vol 34 (5) ◽  
pp. 279-287 ◽  
Author(s):  
Moshe Rosenberg ◽  
Andreas Altemueller
1998 ◽  
Vol 51 (1) ◽  
pp. 1-10 ◽  
Author(s):  
T P GUINEE ◽  
M A FENELON ◽  
E O MULHOLLAND ◽  
B T O'KENNEDY ◽  
N O'BRIEN ◽  
...  

1997 ◽  
Vol 30 (1) ◽  
pp. 35-40 ◽  
Author(s):  
M.A. Drake ◽  
T.D. Boylston ◽  
K.D. Spence ◽  
B.G. Swanson

2003 ◽  
Vol 86 (5) ◽  
pp. 1608-1615 ◽  
Author(s):  
Shakeel Ur Rehman ◽  
N.Y. Farkye ◽  
T. Considine ◽  
A. Schaffner ◽  
M.A. Drake

1993 ◽  
Vol 76 (10) ◽  
pp. 2832-2844 ◽  
Author(s):  
D.L. Anderson ◽  
V.V. Mistry ◽  
R.L. Brandsma ◽  
K.A. Baldwin

2002 ◽  
Vol 68 (4) ◽  
pp. 1778-1785 ◽  
Author(s):  
Jeffery R. Broadbent ◽  
Mary Barnes ◽  
Charlotte Brennand ◽  
Marie Strickland ◽  
Kristen Houck ◽  
...  

ABSTRACT Bitterness is a flavor defect in Cheddar cheese that limits consumer acceptance, and specificity of the Lactococcus lactis extracellular proteinase (lactocepin) is widely believed to be a key factor in the development of bitter cheese. To better define the contribution of this enzyme to bitterness, we investigated peptide accumulation and bitterness in 50% reduced-fat Cheddar cheese manufactured with single isogenic strains of Lactococcus lactis as the only starter. Four isogens were developed for the study; one was lactocepin negative, and the others produced a lactocepin with group a, e, or h specificity. Analysis of cheese aqueous extracts by reversed-phase high-pressure liquid chromatography confirmed that accumulation of αS1-casein (f 1-23)-derived peptides f 1-9, f 1-13, f 1-16, and f 1-17 in cheese was directly influenced by lactocepin specificity. Trained sensory panelists demonstrated that Cheddar cheese made with isogenic starters that produced group a, e, or h lactocepin was significantly more bitter than cheese made with a proteinase-negative isogen and that propensity for bitterness was highest in cells that produced group h lactocepin. These results confirm the role of starter proteinase in bitterness and suggest that the propensity of some industrial strains for production of the bitter flavor defect in cheese could be altered by proteinase gene exchange or gene replacement.


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