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Assessing the Myofibrillar and Connective Tissue Protein Contents and Protein Quality of Beef Tripe

1996; American Chemical Society; Volume: 44; Issue: 9 Linguagem: Inglês

10.1021/jf950262y

1520-5118

George C. Zarkadas, Constantinos D. Karatzas, Constantinos G. Zarkadas,

Meat and Animal Product Quality

The myofibrillar actin content of adult bovine tripe has been determined from the amounts of Nτ-methylhistidine found in acid hydrolysate. Collagen and elastin have also been determined from the amounts of 5-hydroxylysine and isodesmosine present, respectively. The beef tripe contained 13.36% actin and 9.59% myosin, corresponding to 37.9 and 27.1% of the myofibrillar protein (35.3% of the total protein). Beef tripe contained high levels of collagen (20.1%) and elastin (1.0%). Beef tripe provides adequate amounts of all of the essential amino acids (EAA9) ranging from 40.3 to 41.9%, compared to FAO/WHO reference EAA9 pattern value of 33.9% for a 2−5-year-old child, and it is limited only in tryptophan, reflecting the amount of connective tissue proteins present. Evaluation of protein quality of smooth muscles can be based on a knowledge of their digestibility and FAO/WHO amino acid scoring pattern and of their myofibrillar and connective tissue protein contents. Keywords: Smooth muscle; beef tripe; myofibrillar; myosin; actin; collagen; elastin; assessment; protein quality; amino acids; composition