Application of concave induction cooking to improve the texture and flavor of braised pork

Long-term cooking may reduce the eating and nutritional quality attributes of meat products due to excessive oxidation. This study aimed to investigate the feasibility of concave induction to improve the quality of braised pork belly. Pork belly cubes were subjected to concave induction cooking (2000 W) or plane induction cooking (2000 W, traditional) for 60 min, 90 min, 120 min or 150 min. Then texture, fatty acid profile, lipid and protein oxidation, volatile flavor and sensory test in braised meat were evaluated. Compared with traditional method, concave induction cooking showed higher heating performance with shorter time to achieve a setting temperature. Compared with traditional cooking for 150 min, concave induction cooking for 60 min did not only produce a comparable volatile flavor and sensory scores, but also give better quality attributes, including lower hardness, chewiness, thrombogenicity values, PUFA/SFA value, lipid and protein oxidation. E‑nose results showed that samples cooked by concave induction for 60 min and 90 min showed a great similarity to those cooked by plane induction for 150 min. Concave induction cooking for 60 min also showed advantages to retain higher abundances of other volatile compounds including 2-pentylfuran, (E, E)-3,5-octadien‑2- one, 2, 3-octanedione, 2-decahydro‑1,6- dimethylnaphthalene when compared with plane induction cooking for 150 min.

Oxidized Substrates of APEH as a Tool to Study the Endoprotease Activity of the Enzyme

APEH is a ubiquitous and cytosolic serine protease belonging to the prolyl oligopeptidase (POP) family, playing a critical role in the processes of degradation of proteins through both exo- and endopeptidase events. Endopeptidase activity has been associated with protein oxidation; however, the actual mechanisms have yet to be elucidated. We show that a synthetic fragment of GDF11 spanning the region 48–64 acquires sensitivity to the endopeptidase activity of APEH only when the methionines are transformed into the corresponding sulphoxide derivatives. The data suggest that the presence of sulphoxide-modified methionines is an important prerequisite for the substrates to be processed by APEH and that the residue is crucial for switching the enzyme activity from exo- to endoprotease. The cleavage occurs on residues placed on the C-terminal side of Met(O), with an efficiency depending on the methionine adjacent residues, which thereby may play a crucial role in driving and modulating APEH endoprotease activity.

Protein Oxidation in Muscle Foods: A Comprehensive Review

Muscle foods and their products are a fundamental part of the human diet. The high protein content found in muscle foods, as well as the high content of essential amino acids, provides an appropriate composition to complete the nutritional requirements of humans. However, due to their special composition, they are susceptible to oxidative degradation. In this sense, proteins are highly susceptible to oxidative reactions. However, in contrast to lipid oxidation, which has been studied in depth for decades, protein oxidation of muscle foods has been investigated much less. Moreover, these reactions have an important influence on the quality of muscle foods, from physico-chemical, techno-functional, and nutritional perspectives. In this regard, the loss of essential nutrients, the impairment of texture, water-holding capacity, color and flavor, and the formation of toxic substances are some of the direct consequences of protein oxidation. The loss of quality for muscle foods results in consumer rejection and substantial levels of economic losses, and thus the control of oxidative processes is of vital importance for the food industry. Nonetheless, the complexity of the reactions involved in protein oxidation and the many different factors that influence these reactions make the mechanisms of protein oxidation difficult to fully understand. Therefore, the present manuscript reviews the fundamental mechanisms of protein oxidation, the most important oxidative reactions, the main factors that influence protein oxidation, and the currently available analytical methods to quantify compounds derived from protein oxidation reactions. Finally, the main effects of protein oxidation on the quality of muscle foods, both from physico-chemical and nutritional points of view, are also discussed.

Chemical Stability of Proteins in Foods: Oxidation and the Maillard Reaction

Protein is a major nutrient present in foods along with carbohydrates and lipids. Food proteins undergo a wide range of modifications during food production, processing, and storage. In this review, we discuss two major reactions, oxidation and the Maillard reaction, involved in chemical modifications of food proteins. Protein oxidation in foods is initiated by metal-, enzyme-, or light-induced processes. Food protein oxidation results in the loss of thiol groups and the formation of protein carbonyls and specific oxidation products of cysteine, tyrosine, tryptophan, phenylalanine, and methionine residues, such as disulfides, dityrosine, kynurenine, m-tyrosine, and methionine sulfoxide. The Maillard reaction involves the reaction of nucleophilic amino acid residues with reducing sugars, which yields numerous heterogeneous compounds such as α-dicarbonyls, furans, Strecker aldehydes, advanced glycation end-products, and melanoidins. Both protein oxidation and the Maillard reaction result in the loss of essential amino acids but may positively or negatively impact food structure and flavor. Expected final online publication date for the Annual Review of Food Science and Technology, Volume 13 is March 2022. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

Prevention of Protein Oxidation in Chicken Meat during Chilled Storage Using Chitosan Gelatin Films with Green Tea Extracts

In present study, the usability of chitosan and gelatin (1:1) films incorporated with green tea extract (GTE) to improve the shelf life of the chicken meat stored in chilled condition was evaluated. The extract of green tea was evaluated for its phenolic content, antioxidant activity and ferric ion chealating ability. The ChGel films possessed antimicrobial activity and inactivated approximately 3 log cfu/ ml of K. pneumoniae, S. typhi var. Weltevreden, S. typhi var. Oslo, Y. enterocolitica, E. feacalis, B. cereus, E. coli and S. aureus in 3 hours. Incorporation of GTE influenced the optical and mechanical properties of the films. Chicken samples without films were observed to be microbiologically safe for not more than 6 days, while ChGel and ChGel-GTE films improved the microbial safety of chicken samples till day 13. ChGel-GTE films also prevented lipid peroxidation in samples as evident by TBARS value (day 10: control: 1.14; ChGel-GTE: 0.21 mg MDA eq/kg). Protein oxidation during chilled storage of chicken was also prevented by ChGel-GTE by inhibiting protein carbonylation, loss of free thiols groups in protein and lowering the number of disulphde bonds. This study supports use of ChGel films with GTE for enhancing the safety of stored chicken meat not only by maintaining the microbial quality of the samples but also preventing oxidative changes which can hamper the functional, nutritional and sensorial properties.

Determination of Protein Oxidation in Aquaculture Feed

The aim of this research was to develop reliable, easy-to-perform and cheap method for measuring protein oxidation in complex samples such as aquaculture feed within various protein sources. For that purpose modified 2,4-dinitrophenylhydrazyne (DNPH)-based method for quantification of protein carbonyls was employed, while the method modification was consisted of using different solutions for the extraction, time of protein extraction and concentration of trichloracetic acid (TCA) for protein precipitation. It was found that extraction during night, higher TCA concentration and the use of 0.5 M KCl extraction solution resulted in the highest protein amount measured by Lowry method and 280 nm protein estimation. On the other hand, the lowest protein yield was obtained by using distillated water for the extraction. Furthermore, the lowest amount of protein carbonyls was in the case when extraction was performed with distilled water (DW), while the highest content of protein carbonyls were reached with 0.15 M KCl and 0.5 M KCl extraction solutions. It was observed that the amount of carbonyls compounds were increasing during storage under accelerated conditions, and in comparison to the original (unmodified) method, the modified method for measuring protein oxidation resulted in the higher amount of carbonyls during the all points of storage.

Effect of Dietary Curcumin Supplementation on Duck Growth Performance, Antioxidant Capacity and Breast Meat Quality

This study aimed at examining the effects of curcumin supplementation on growth performance, antioxidant capacity, and meat quality of ducks. To investigate these effects, 600 healthy ducks were randomly assigned to four treatment groups with 10 replicates pens, and each pen contained 15 ducks. Ducks were fed a diet containing curcumin at levels of 0, 300, 400, and 500 mg kg−1 in different groups. The results demonstrated that curcumin supplementation is beneficial to the growth performance (p < 0.05) of ducks and antioxidant capacity (p < 0.05) of duck meat. In addition, dietary curcumin raised the meat quality of ducks, improving the meat color, increasing water-holding capacity, and inhibiting lipid and protein oxidation. In conclusion, the present study provides important insights into both the nutrient and qualities of ducks, finding that a dietary inclusion of 400–500 mg/kg of curcumin (kg−1) has the greatest effect.