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The effect of the addition of native starch (S) and modified starches (distarch phosphate (SP), acetylated distarch phosphate (AP), and starch acetate (SA)) in emulsion-type sausage on the digestion process of meat protein was studied in this work. The addition of native and modified starches reduced the release of -NH 2 during the simulated gastric digestion stage, whereas the addition of SA increased the total release of -NH 2 after the whole digestion. Peptidomic analysis revealed that the presence of starch decreased the release of peptides in the gastric digestion. The presence of starch reduced the stability of the digests but increased the viscosity of the gastric digestive fluid, which should largely be responsible for the decreased gastric digestibility of meat protein. These results highlighted the physical properties of digests as a key factor affecting the gastric digestion process of meat protein and provided guidance for the application of starches in meat products.

Existing reviews address bioactive peptides of meat proteins; however, comprehensive reviews summarizing the released sequences and their corresponding parent meat proteins in the digesta are limited. This review explores the bioactive peptides released during the in vitro gastrointestinal (GI) digestion of meat, connecting with parent proteins. The primary bioactivities of meat-derived peptides include angiotensin-converting enzyme (ACE) and dipeptidyl peptidase (DPP)-IV inhibition and antioxidant effects. Myofibrillar, sarcoplasmic, and stromal proteins play a significant role in peptide release during digestion. The release of bioactive peptides varies according to the parent protein and cryptides had short chains, non-toxicity, and great bioavailability and GI absorption scores. Moreover, the structural stability and bioactivities of peptides can be influenced by the digestive properties and amino acid composition of parent proteins. Investigating the properties and origins of bioactive peptides provides insights for enhancing the nutritional quality of meat and understanding its potential health benefits., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Replacing animal fat with vegetable oil occurred extensively in the meat products, but whether these replacements will affect the nutrition of meat protein was seldom revealed. Effect of substitution of back fat (BF) by vegetable oils or their oleogels in emulsion-type sausage on the digestion process of meat protein was investigated. Replacement of BF with vegetable oils and their oleogels decreased the G'/G" values of meat paste, and oleogels largely weakened the structure of sausages. The substitution significantly reduced the liberation of -NH 2 during the initial gastric and intestinal digestion, and resulted in bigger digests in CLSM images. The reduced gastric digestibility induced by substitution was shown to be related to the reduced stability of gastric digests, which can be attributed to the larger particle size and reduced viscosity of digests. These results highlighted stability of digests as a key point changing the digestion process of meat protein., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Meat is a valuable protein source with a balanced composition of essential amino acids and various nutrients. This review aims to identify methods to improve digestion of meat proteins, as well as evaluate the digestive characteristics of infants and the elderly. Immature digestive conditions in infants, including a high gastric pH and low protease concentration, can hinder protein digestion, thus resulting in inhibited growth and development. Likewise, gastrointestinal (GI) tract aging and chronic health problems, including tooth loss and atrophic gastritis, can lead to reduction in protein digestion and absorption in the elderly compared with those in young adults. Moderate heating and several non-thermal technologies, such as aging, enzymatic hydrolysis, ultrasound, high-pressure processing, and pulsed electric field can alter protein structure and improve protein digestion in individuals with low digestive capacity., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

The elderly population will increase sharply in the future, along with an emerging range of specific nutritional needs that include adapted food. We aimed to develop a workflow to study the fate of a food, objectify the bioavailability of nutrients in the case of the digestive physiology of the elderly, and model the fate of proteins in the stomach. Pork frankfurters were subjected to in vitro normal and deficient mastication and gastric digestion, mimicking adult and elderly food oral and digestive processing. Swallowable food boluses were characterized for granulometric and rheological properties. Biochemical analyses were conducted on the bolus and on the digesta. Macronutrients, label-free peptide quantification and identification were performed, and modeling was applied to protein digestion kinetics. After deficient mastication, the food bolus was harder with more large particles, lower free iron release and more protein oxidation. The amount of peptides released in the stomach progressively increased, but to a lower extent for the elderly digestive condition and irrespective of masticatory efficiency. 592 peptides were identified from 67 proteins. Different trajectories were observed for adult and elderly digestive conditions, and two groups of meat proteins were identified based on the rate of hydrolysis. Designing suitable foods requires in vitro tools to evaluate the possible benefit for the elderly. Besides the well-known notion of Food Oral Processing (FOP), our work broadens the concept by extending oral activity to digestion when working in a nutritional context. This new concept is named Food Oral and Digestive Processing, FODP.

Nitrosation can occur during meat digestion due to the physicochemical conditions of the stomach (low pH and reducing conditions). The aim of the present study was to elucidate the link between the nitrosation of proteins from beef meat and their digestibility by comparing cooked meat digested with and without the addition of nitrite. To do this, a dynamic in vitro artificial digestive computer-controlled system (DIDGI®) was used to reflect human gastro-intestinal conditions. Peptides and proteins from gastrointestinal digestion were identified by high-resolution LC-MS/MS mass spectrometry. The results showed a dynamic digestion pattern of meat proteins according to their cellular localization. A combined effect of the digestive compartment and the addition of nitrite was established for the first time on peptides profile, linking the nitrosation of proteins and their digestibility., (Copyright © 2018 Elsevier Ltd. All rights reserved.)

Background: Protein quality assessment through the Digestible Indispensable Amino Acid Score requires accurate measurements of true ileal protein and amino acid digestibility, for which a dual isotope technique was recently developed. However, the ileal digestibility of indispensable amino acids (IAA) in humans from high-quality proteins is not well known., Objective: The aim of this study was to intrinsically label hen's egg and meat protein by the use of uniformly 2H-labeled amino acids, and to measure their true ileal indispensable amino acid (IAA) digestibility via the dual isotope method in humans., Design: 2H-labeled lyophilized boiled egg white protein, whole boiled egg, and cooked meat were obtained from layer hens (BV-300) administered a uniformly 2H-labeled amino acid mix orally for 35 d with their daily feed. The ileal IAA digestibility of these proteins was determined with reference to digestibility of previously characterized [U-13C]spirulina in a dual tracer method in healthy Indian subjects whose intestinal health was measured by the plasma kynurenine-to-tryptophan (KT) ratio., Results: All subjects had normal KT ratios. The mean ± SD true ileal IAA digestibility of 2H-labeled egg white protein, whole boiled egg, and cooked meat was 86.3% ± 4.6%, 89.4% ± 4.5%, and 92.0% ± 2.8%, respectively. Leucine digestibility correlated with the KT ratio (r = -0.772; P = 0.009)., Conclusions: Uniformly 2H-labeled hen's egg and meat protein can be used to measure ileal IAA digestibility by the dual isotope tracer approach in humans. The mean IAA digestibility values for these high-quality proteins in the healthy Indians studied were similar to values obtained in earlier human and animal experiments. Leucine digestibility in these meal matrices correlated with the KT ratio, but this aspect needs further evaluation. This trial was registered at the Clinical Trials Registry of India (http://ctri.nic.in) as CTRI/2018/03/012265.