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1.
Food Chem ; 109(1): 42-53, 2008 Jul 01.
Artigo em Inglês | MEDLINE | ID: mdl-26054263

RESUMO

Physicochemical and rheological properties of myosin from Atlantic cod and burbot during acid-induced gelation at room temperature (22-23°C) by d-gluconic acid-δ-lactone (GDL) were monitored. Turbidity and particle size of both myosins increased and salt soluble content decreased when pH decreased, suggesting the formation of protein aggregates caused by acidification. The formation of disulphide bonds in myosin gelation was induced by acid. Ca(2+)-ATPase activity of myosin decreased (p<0.05), while surface hydrophobicity increased during acidification (p<0.05). Furthermore, the decreases in maximum transition temperature (Tmax) and the denaturation enthalpies (ΔH) were found in both myosins. During acidification, the increases in storage modulus (G') and loss modulus (G″) of myosin were observed (p<0.05), revealing the formation of elastic gel matrix. Thus, gelation of myosin from Atlantic cod and burbot could take place under acidic pH via denaturation and aggregation. However, myosin from Atlantic cod was generally more favourable to gelation than was burbot myosin.

2.
Meat Sci ; 66(3): 579-88, 2004 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-22060867

RESUMO

Changes in composition and functional properties of proteins during fermentation of Nham, a Thai-fermented sausage, were studied. An alkaline-soluble fraction constituted a major protein component of Nham. The amount of each protein fraction in Nham varied, depending on the fermentation time. As fermentation proceeded, the progressive decrease in sarcoplasmic and myofibrillar protein fractions was accompanied by an increase in the alkaline-soluble fraction and non-protein constituents (P<0.05). Slow pH lowering to pH 4.6 during fermentation as a result of bacterial growth and accumulation of lactic acid affected the molecular conformation of the muscle proteins and resulted in changes in protein functional properties. The acid produced resulted in changes in solubility, water-binding capacity, textural properties, and color characteristics. Proteolysis of Nham proteins occurred during fermentation, resulting in increases in TCA-soluble peptides and free α-amino acids, which may contribute to the taste and aroma of Nham.

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