Insights into Digestibility and Peptide Profiling of Beef Muscle Proteins with Different Cooking Methods

Abstract

This study aimed to investigate theeffects of sous vide (SV), boiling (BO), and roasting (RO) on beef protein digestibility and peptide profiling in simulated gastrointestinal digestion. The results indicated that beef samples treated with SV had higher (p < 0.05) gastrointestinal digestibility (34.97%) than those treated with BO (27.59%) and RO (24.36%). Furthermore, SV (2450) resulted in more types of peptides released during gastrointestinal digestion than BO (2077) and RO (1896) and a higher proportion of 400−1200 Da peptides. The significant increase of carbonyl content, the decrease of sulfhydryl content, and the formation of covalent bonds coupled with the transformation of protein secondary structure from α-helix to β-sheet suggested that excessive protein oxidation and aggregation occurred in BO and RO samples. These changes in BO and RO samples might explain the decreased protein digestibility and peptide release in gastrointestinal digestion. Thus, SV is a promising cooking method to improve beef protein digestibility.

Effect of Different Processing Methods on Quality, Structure, Oxidative Properties and Water Distribution Properties of Fish Meat-Based Snacks

“…However, the increased protein oxidation in baking after frying could be attributed to long cooking time along with higher temperature, which are responsible for protein oxidation, as reported previously [6]. The increased oxidation by frying has also been reported by previous studies [9]. On the other hand, the lowest protein carbonyl content in microwave heating endorses the suitability of microwave heating, which was for less time, in terms of safety point of view.…”

“…Heat disrupts the native conformation of polypeptides, which hold the molecules together, resulting the increase in thermal motion, loss of secondary and tertiary structure [6] and rupturing the intermolecular forces, e.g., electrostatic or non-polar interaction and disulfide bonds [8]. Further, once proteins are unfolded in response of thermal processing, aggregation of proteins occur and scramble the disulfide bonding, resulting in side chain modifications [9], which cross link with other polypeptides that are exposed to oxidation. In addition, processing methods have significant influence in terms of structural modification [6], textural changes [10], water distribution [11], microstructural changes [12] and even oxidative changes [13].…”

Effect of Malondialdehyde on the Digestibility of Beef Myofibrillar Protein: Potential Mechanisms from Structure to Modification Site

“…Protein digestibility was determined by degree of hydrolysis (DH) following our previous work [ 25 ]. Briefly, 75 μL of the digestion was precipitated with an equal volume of TCA (24%) in ice water for 30 min.…”

Effect of ultrasonic treatment on the structure and functional properties of mantle proteins from scallops (Patinopecten yessoensis)

“…Total SH and free SH were obtained with DTNB rate colorimetry [21] . For the total SH, scallop mantle protein solution (1 mg/mL, 0.5 mL) was mixed with 5 mL of buffer solution (10 mM EDTA, 8 M urea, 20 mM Tris–HCl, pH 6.0).…”