Chicken marinated with yogurt is more flavorful, but less tender and less juicy and appears darker than control.
Why???
More flavorful and appears darker than control.
Yogurt contains:
- sweeteners provides the sweet taste
- lactic acid bacteria as starter culture for fermentation
Yogurt marinated meat has higher flavor. This may be due to the sweeteners present in yogurt. When poultry is cooked, flavor develops from sugar and amino acid interactions. This flavor development is due to Maillard reaction. The Maillard reaction occurs due to the denatured proteins on the surface of the meat interact with the sugars present which produces the "meaty" flavor and changes the color. This explains why yogurt marinade meat appears browner.
Less tender and less juicy than control.
The less tenderness is due to the high amount of LAB in yogurt creates a low pH and high LAB counts. This low pH causes protein in muscle to coagulate and contracts, forcing the water out of the meat. But if the protein is in a very acidic marinade, such as in our yogurt marinade, the protein bonds tighten, water is squeezed out, and the tissue becomes tough. It was also reported that meat with low ph is likely to be poorer eating quality as the enzymes involved in post mortem tenderization are inhibited by the acidification.
A related factor influencing water binding, and juiciness is meat pH. The rate and extent of pH decline during rigor development in muscle can influence myofibrillar protein functionality, thereby altering meat tenderness, color, WHC, and meat protein binding ability. As rigor develops, myosin combines with actin to form actomyosin. Actomyosin, although not a poor water binder, is not as good as myosin and not as readily solubilized. Additionally, lactic acid accumulates and muscle pH drops to 5.6 or 5.7 in normal tissue. As pH declines during rigor, there is an efflux of fluid from the myofibrillar space caused by the decrease in negative electrostatic repulsion between filaments. As rigor is resolved, the muscle pH approaches the isoelectric point for the myofibrillar proteins, which is approximately 5.1. Decreased WHC occurs because actin and myosin are near their isoelectric point in postrigor meat, and the net charges on the protein will be a minimum, as will space between filaments for water to be held or bound
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