Enzymatic Digestion of Calf Fleshing Meat By-Products: Antioxidant and Anti-Tyrosinase Activity of Protein Hydrolysates, and Identification of Fatty Acids

Abstract

The food waste reduction through an efficient recovery of its valuable building molecules has become an important topic with a positive effect on the economy and the environment. In this work, the revalorization of slaughterhouse calf fleshing meat through its enzymatic hydrolysis is proposed. The proteolytic activity of 11 enzymes was initially screened and the four most efficient enzymes (papain, trypsin, pancreatin, and bromelain) were selected. The molecular profiling of the different protein/peptide fractions by the Linear Trap Quadrupole-OrbiTrap technique showed compositional differences due to the specificity of the enzymes’ cleavage sites. In order to find a potential reuse of these hydrolysates, the analysis of antioxidant and, for the first time on fleshing meat hydrolysates, of anti-tyrosinase activities, was performed. Papain-digested samples were those showing the highest inhibition activity of tyrosinase enzyme (55.6%) as well as the highest antioxidant activity (3.52 g TEAC/L). In addition, the composition analysis of the lipid fraction was performed. The mono-unsaturated fatty acids resulted to be the most abundant lipid in all the samples with the exception of pancreatin-treated hydrolysates in which poly-unsaturated fatty acids were predominant. The present results seemed to support a possible valorization of isolated fractions from calf fleshing by-products, as food or feed ingredients, by the implementation of fraction isolation within the meat-processing pipeline.

Antioxidant, Anti-Tyrosinase, and Wound-Healing Capacities of Soy Protein Hydrolysates Obtained by Hydrolysis with Papaya and Cantaloupe Juices Showing Proteolytic Activity

“…Protein hydrolysates obtained by enzymes of plant origin have been analysed for their inhibition of tyrosinase activity. For example, the hydrolysates of calf fleshing by-products obtained by papain and bromelain exhibited inhibitory effects on tyrosinase activity [Tedeschi et al, 2021]. The improvement of anti-tyrosisnase activity in the protein hydrolysates is possibly contributed by peptides as products of the hydrolysis process [Hu et al, 2022].…”

The Characterization of Subcutaneous Adipose Tissue in Sunit Sheep at Different Growth Stages: A Comprehensive Analysis of the Morphology, Fatty Acid Profile, and Metabolite Profile

“…SFAs were the primary FAs in the SAT. Due to the hydrogenation process of UFAs catalyzed by rumen microflora, ruminant animals exhibit significantly reduced levels of PUFAs [32,33]. The PUFA/SFA, as well as that of n-6/n-3, are two important parameters in the evaluation of meat lipids.…”

Optimization of a Novel Tyrosinase Inhibitory Peptide from Atrina pectinata Mantle and Its Molecular Inhibitory Mechanism

“…The two enzymes with the highest DH-papain and neutral protease-produced enzymatic products with good tyrosinase inhibitory activity, with inhibition rates of 81.18 ± 0.56% and 75.48 ± 3.19%, respectively. Papain has a wider specificity than trypsin in that it cuts the carboxyl side of lysine and arginine residues as well as aromatic amino acid residues in the peptide chain, leaving the functional amino acid residues exposed on the terminal side of the peptide chain [29], so that the gelatinized peptide obtained has a higher inhibitory activity against tyrosinase. Papain was selected as the optimal enzyme based on the experimental results and the economic benefits.…”