Food ingredients commonly undergo heat treatment. Meat, in particular, is typically consumed after some form of heating, such as boiling or roasting. Heating of meat can introduce a wide range of structural changes in its proteinaceous components. At the 3-dimensional structural level, meat proteins may denature and form aggregates upon heating. At the molecular level, primary structure (amino acid residue) alterations reported in cooked meat include protein carbonylation, modification of aromatic residues, and the formation of Maillard reaction products. Identification of these modifications is essential for determining the mechanism of thermal processing of meat and allowing better control of the nutritional and functional properties of products. This article reviews and summarizes the current state of understanding of protein modifications at the molecular level in commonly consumed mammalian food. In addition, relevant case studies relating to characterization of heat-induced amino acid residue-level modifications in other biological materials such as milk and wool are discussed to provide complementary insights.
Defined as meat cultured in a laboratory within a bioreactor under controlled artificial conditions, in vitro meat is a relatively recent area that has opened a whole universe of possibilities and opportunities for the meat sector. With improved chemical and microbial safety and varied options, in vitro meat has been proposed as a green, healthy, environmentally friendly, and nutritionally better product that is free from animal suffering and death. Cell culture and tissue culture are the most probable technologies for the development of this futuristic muscle product. However, there are many challenges in the production of a suitable product at an industrial scale under a sustainable production system and a great body of research is required to fill the gaps in our knowledge. Many materials used in the product development are novel and untested within the food industry and demand urgent regulatory and safety assessment systems capable of managing any risks associated with the development of cultured meat. The future of this product will depend on the actions of governments and regulatory agencies. This article highlights emerging biotechnological options for the development of cultured meat and suggests ways to integrate these emerging technologies into meat research. It considers the problems and possibilities of developing cultured meat, opportunities, ethical issues as well as emerging safety and regulatory issues in this area.
The photosynthate costs of processes (amino acid and protein synthesis and turnover, and pH regulation) associated with the utilization of nitrate (NO $ − ), ammonium (NH % + ) or glutamine (Gln) for plant growth were estimated. Based on these estimates, the effects of these forms of nitrogen (N) on the carbon balance of plants and on shoot-root biomass allocation were evaluated. The results indicated that NO $ − as an N source for plant growth is not substantially more expensive to utilize than either NH % + or Gln, particularly in the long term when costs due to protein turnover dominate the total costs of N utilization. It is also suggested that the photosynthate use in processes associated with N assimilation has little impact on the carbon balance of plants, and hence on shoot-root biomass allocation.
Pulsed electric field (PEF) is a novel non-thermal technology that has recently attracted the attention of meat scientists and technologists due to its ability to modify membrane structure and enhance mass transfer. Several studies have confirmed the potential of pulsed electric field for improving meat tenderness in both pre-rigor and post-rigor muscles during aging. However, there is a high degree of variability between studies and the underlying mechanisms are not clearly understood. While some studies have suggested physical disruption as the main cause of PEF induced tenderness, enzymatic nature of the tenderization seems to be the most plausible mechanism. Several studies have suggested the potential of PEF to mediate the tenderization process due to its membrane altering properties causing early release of calcium ions and early activation of the calpain proteases. However, experimental research is yet to confirm this postulation. Recent studies have also reported increased post-mortem proteolysis in PEF treated muscles during aging. PEF has also been reported to accelerate curing, enhance drying and reduce the numbers of both pathogens and spoilage organisms in meat, although that demands intense processing conditions. While tenderization, meat safety and accelerated curing appears to be the areas where PEF could provide attractive options in meat processing, further research is required before the application of PEF becomes a commercial reality in the meat industry. It needs to deal with carcasses which vary biochemically and in composition (muscle, fat, and bones). This review critically evaluates the published reports on the topic with the aim of reaching a clear understanding of the possible applications of PEF in the meat sector in addition to providing some insight on critical issues that need to be addressed for the technology to be a practical option for the meat industry.
The tenderization process, which can be influenced by both pre-and post-slaughter interventions, begins immediately after an animal's death and is followed with the disruption of the muscle structure by endogenous proteolytic systems. The post-slaughter technological interventions like electrical stimulation, suspension methods, blade tenderization, tumbling, use of exogenous enzymes, and traditional aging are some of the methods currently employed by the meat industry for improving tenderness. Over the time, technological advancement resulted in development of several novel methods, for maximizing the tenderness, which are being projected as quick, economical, nonthermal, green, and energy-efficient technologies. Comparison of these advanced technological methods with the current applied industrial methods is necessary to understand the feasibility and benefits of the novel technology. This review discusses the benefits and advantages of different emerging tenderization techniques such as hydrodynamic-pressure processing, high-pressure processing, pulsed electric field, ultrasound, SmartStretch TM , Pi-Vac Elasto-Pack R system, and some of the current applied methods used in the meat industry.
Protein and peptide oxidation is a key feature in the progression of a variety of disease states and in the poor performance of protein-based products. The present work demonstrates a mass spectrometry-based approach to profiling degradation at the amino acid residue level. Synthetic peptides containing the photosensitive residues, tryptophan and tyrosine, were used as models for protein-bound residue photodegradation. Electrospray ionisation tandem mass spectrometry (ESI-MS/MS) was utilised to characterise and provide relative quantitative information on the formation of photoproducts localised to specific residues, including the characterisation of low abundance photomodifications not previously reported, including W + 4O modification, hydroxy-bis-tryptophandione and topaquinone. Other photoproducts observed were consistent with the formation of tyrosine-derived dihydroxyphenylalanine (dopa), trihydroxyphenylalanine, dopa-quinone and nitrotyrosine, and tryptophan-derived hydroxytryptophan, dihydroxytryptophan/N-formylkynurenine, kynurenine, hydroxyformylkynurenine, tryptophandiones, tetrahydro-beta-carboline and nitrotryptophan. This approach combined product identification and abundance tracking to generate a photodegradation profile of the model system. The profile of products formed yields information on formative mechanisms. Profiling of product formation offers new routes to identify damage markers for use in tracking and controlling oxidative damage to polypeptides.
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