Digestion is the first step in the metabolic fate of ingested food proteins; in view of its significant physiological and pathological consequences, the digestion process frequently has to be taken into consideration. In this paper, an improved in vitro multienzymatic digestibility assay has been used to evaluate protein degradation in lamb meat samples, that is, raw, steam-cooked, homogenized (strained), and commercially available freeze-dried meat, all from the same processing chain. Our data indicate that enzymatic attack is strongly affected by heat treatment as shown in steam-cooked meat samples. On the other hand, homogenization and freeze-drying processes are able to partially reverse the phenomenon, thus improving peptide and amino acid release. Data on modification of SDS-PAGE protein pattern during the multienzymatic assay are also reported.
Digestibility of technologically treated lamb meat samples evaluated by an in vitro multienzymic method / P. Restani, A. R. Restelli, A. Capuano, C. L. Galli. - In: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. - ISSN 0021-8561. - 40:6(1992), pp. 989-993.
Digestibility of technologically treated lamb meat samples evaluated by an in vitro multienzymic method
P. RestaniPrimo
;C. L. GalliUltimo
1992
Abstract
Digestion is the first step in the metabolic fate of ingested food proteins; in view of its significant physiological and pathological consequences, the digestion process frequently has to be taken into consideration. In this paper, an improved in vitro multienzymatic digestibility assay has been used to evaluate protein degradation in lamb meat samples, that is, raw, steam-cooked, homogenized (strained), and commercially available freeze-dried meat, all from the same processing chain. Our data indicate that enzymatic attack is strongly affected by heat treatment as shown in steam-cooked meat samples. On the other hand, homogenization and freeze-drying processes are able to partially reverse the phenomenon, thus improving peptide and amino acid release. Data on modification of SDS-PAGE protein pattern during the multienzymatic assay are also reported.Pubblicazioni consigliate
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