ABSTRACT. Aroma properties of twenty‐three branched‐chain, odd‐numbered, or unsaturated fatty acids which had each been dispersed in acidic aqueous media (pH 2.0) were evaluated. Aroma threshold values were determined using approximately 95 judges for assessing the presence of aromas over dilutions of each fatty acid. Qualitative aroma threshold values for individual fatty acids ranged from 0.006 to 82.4 ppm in the acidic solutions, and 4‐ethyloctanoic acid exhibited the lowest threshold of the group tested. Qualitative aroma assessments of dilutions of each fatty acid showed a wide range of unique aroma properties. Fatty acids exhibiting branching at the 4‐position had goaty/muttony/sheepy aroma notes as did other fatty acids containing 8‐carbon chain structures. Cheese‐like aromas were associated with the shorter branched‐chain fatty acids.

Twenty cows were used in a randomized block design experiment for 6 wk to determine the influence of feeding partial ruminally inert Ca salts of palm and fish oil (Ca-PFO), alone or in combination with extruded full-fat soybeans or soybean oil, on milk fatty acid (FA) methyl esters composition and consumer acceptability of milk and Cheddar cheese. Cows were fed either a diet containing 44% forage and 56% concentrate (control) or a diet supplemented with 2.7% Ca-PFO (FO), 5% extruded full-fat soybeans + 2.7% Ca-PFO (FOESM), or 0.75% soybean oil + 2.7% Ca-PFO (FOSO). Total dietary FA content in the control, FO, FOESM, and FOSO diets were 4.61, 6.28, 6.77, and 6.62 g/100 g, respectively. There was no difference in nutrient intake, milk yield, or milk composition among treatments. Conjugated linoleic acid (CLA) C(18:2) cis-9, trans-11 isomer, C(18:1) trans-11 (VA), and total n-3 FA in milk from cows on the control, FO, FOESM, and FOSO treatments were 0.56, 1.20, 1.36, and 1.74; 3.29, 4.66, 6.34, and 7.81; 0.62, 0.69, 0.69, and 0.67 g/100 g of FA, respectively. Concentrations of CLA, VA, and total n-3 FA in cheese were similar to milk. A trained sensory panel detected no difference in flavors of milk and cheese, except for acid flavor below a slightly perceptible level in cheese from all treatments. Results suggest that feeding Ca-PFO alone or in combination with extruded full-fat soybeans or soybean oil enhanced the CLA, VA, total unsaturated and n-3 FA in milk and cheese without negatively affecting cow performance and consumer acceptability characteristics of milk and cheese.

The quality of ground beef stored in high-oxygen modified atmosphere packaging (MAP) (80% O 2 and 20% CO 2 ) was evaluated and compared to controls stored in oxygen-impermeable chubs. Patties were formed from the stored ground meat at d 1, 6, and 10. Color, microbial load, thiobarbituric acid (TBA) number, and sensory acceptability were measured. Patties from both treatments bloomed to red with a* values > 16. Aerobic plate counts increased to 9 × 10 5 CFU/g by 10 d storage, but were not different (p < 0.05) between treatments. TBA number of highoxygen samples increased to 2.1 after 10 d, compared to 0.8 for controls. The flavor of samples in high-oxygen were rated less desirable after 6 or 10 d.

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 ␣ S1 -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.Proteolysis and its secondary reactions play a major role in the maturation of Cheddar and many other bacterium-ripened cheese varieties (16). Proteolysis in Cheddar cheese is a complex process that involves endogenous milk enzymes, coagulant, and microbial proteinases and peptidases. Hydrolysis of intact casein (CN) is catalyzed almost exclusively by the added coagulant and endogenous milk enzymes, while proteinases and peptidases from Lactococcus lactis starter bacteria and adventitious (nonstarter) lactic acid bacteria are responsible for the production of water-soluble peptides and free amino acids (17). The contribution of individual enzymes in the cheese matrix to this process will also be influenced by specificity, relative activity, stability in the cheese matrix, and in the case of intracellular enzymes, access to appropriate substrates.In many bacterium-ripened cheeses, the L. lactis cell envelope-associated proteinase (lactocepin, EC 3.4.21.96) is the most important microbial enzyme for the conversion of largemolecular-weight (water-insoluble) peptides produced by coagulant or plasmin into the small water-soluble peptides needed for flavor development (10,17,35). Lactocepin is a 180-to 190-kDa membrane-anchored enzyme that belongs to the subtilisin family of serine proteases. Although lactocepins exhibit more than 98% amino acid sequence identity, purified enzymes may be differentiated by their relative affinity and specificity for individual CNs (23). Genetic studies showed that most differences in lactocepin specificity could be traced to amino acid substitutions in the enzyme substrate-binding regions, and this ...