Food Protein Chemistry: An Introduction For Foo...
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For CPG companies and food manufacturers to win market share in this fast-growing segment over the long term, they must invest in the capabilities required to develop and manufacture the most promising alternative-protein products.
Animal protein will likely continue to dominate the market driven by key advantages such as customer familiarity. However, there is room at the table for plant-based products as evidenced by growing, shifting customer concerns around traditional meat protein. Companies are already investing in alternative proteins technology and will continue to do so in the coming years. And players that can market high-end products made from soy protein are likely to capture the largest margins. For CPG companies to win market share in the long term, they must place their bets and invest in the capabilities needed to meet their marketing strategy and the target consumer segments. Overall, alternative proteins present an exciting development for the entire food industry.
Peptide mimicking of β-strands and β-sheets. β-sheets and β-strands represent another class of protein secondary structures, based on turn mimics. The modification of peptides to stabilize β-sheets is usually achieved by the introduction of D-amino acids, such as D-Pro, to form a turn structure in the sequence. D-Pro-L-Pro templates are a well-known scaffold for stabilizing antiparallel β-hairpins in several successful PPI inhibitors188,189. Macrocyclization or amyloid beta-sheet mimics have also been applied to create β-sheets and β-strand structures190,191,192,193.
The practice of isolating peptide drugs from natural sources can be traced back to the 1920s, when insulin was first isolated from livestock pancreata and used to treat diabetes205,206, saving hundreds of thousands of lives. The pioneering success of insulin led to increasing public enthusiasm for peptide therapeutics, and several other animal-derived peptide drugs subsequently successfully entered clinical use, such as adrenocorticotropic hormone207 and calcitonin208. Non-ribosomally synthesized peptides represent another important family of natural sources for identifying and producing peptides with therapeutic potential, as exemplified by vancomycin and cyclosporin. Unlike ribosomally synthesized peptides or proteins, the synthesis of non-ribosomally synthesized peptides is controlled by clusters of genes encoding non-ribosomal peptide synthetases rather than the endogenous translational machinery, leading to the production of structurally and functionally diverse peptides, and allowing these molecules to overcome the inherent limitations of common peptide drugs. Venoms and toxins are recognized as valuable natural sources as starting points for identifying bioactive peptides208,209,210, and other natural sources, such as cyclotides and lantipeptides have also been studied and exploited211,212,213. Enzymatic synthesis is suitable for the synthesis of short peptides, such as dipeptides and tripeptides, and enzymatically synthesized peptides have been successfully applied for the production of food additives, pharmaceuticals, and agrochemicals. Fermentation has been well-documented as an eco-friendly approach for producing bioactive peptides, such as in the manufacture of cyclosporine214. Recombinant DNA technology enables the production of peptides and proteins with defined sequences and homogeneity. This approach is particularly useful for manufacturing long or complicated peptides with multiple disulfide bonds, which can otherwise be difficult to synthesize chemically. Human insulin and growth hormone are representative examples of the many available peptide drugs made using recombinant DNA technology. In addition, recombinant DNA technology can be combined with genetic code expansion and other novel technologies to introduce desired functional groups into the molecules via the incorporation of unnatural amino acids, as discussed below. Semi-synthesis provides a flexible approach for producing large bioactive polypeptides by linking synthetic peptides and recombinant DNA-expressed peptides215,216,217, and is a particularly useful approach when multiple artificial modifications are needed.
to foster technological advances in plant/agricultural biotechnology (e.g., crop improvement, nutraceuticals, bioenergy, transgenic plants, phytoremediation), microbial and insect biotechnology (metabolic engineering and synthetic/systems biology of bacteria, fungi, insects, yeasts and algae in the context of fermentation/bioproduction, biocatalysis, bioremediation, biodegradation), food and flavor biotechnology (biotransformations/microbiology and metabolic aspects of food/beverage systems), and protein and enzyme technology (recombinant proteins/enzymes, cell-free protein expression systems, and biocatalysis using immobilized enzymes).
Most dietary niacin is in the form of nicotinic acid and nicotinamide, but some foods contain small amounts of NAD and NADP. The body also converts some tryptophan, an amino acid in protein, to NAD, so tryptophan is considered a dietary source of niacin.
Table 1 lists the current RDAs for niacin as mg of niacin equivalents (NE) [2]. The FNB defines 1 NE as 1 mg niacin or 60 mg of the amino acid tryptophan (which the body can convert to niacin). Niacin RDAs for adults are based on niacin metabolite excretion data. For children and adolescents, niacin RDAs are extrapolated from adult values on the basis of body weight. The AI for infants from birth to 6 months is for niacin alone, as young infants use almost all the protein they consume for growth and development; it is equivalent to the mean intake of niacin in healthy, breastfed infants. For infants aged 7-12 months, the AI for niacin is in mg NE and is based on amounts consumed from breast milk and solid foods.
Food is any substance normally eaten or drunk by living things. The term food also includes liquid drinks. Food is the main source of energy and of nutrition for animals, and is usually of animal or plant origin. There are 4 (four) basic food energy sources: fats, proteins, carbohydrates and alchol.
Protein nutrition in humans In terms of human nutritional needs, proteins come in two forms: complete proteins contain all eight of the amino acids that humans cannot produce themselves, while incomplete proteins lack or contain only a very small proportion of one or more. Humans' bodies can make use of all the amino acids they extract from food for synthesizing new proteins, but the inessential ones themselves need not be supplied by the diet, because our cells can make them ourselves. When protein is listed on a nutrition label it only refers to the amount of complete proteins in the food, though the food may be very strong in a subset of the essential amino acids. Animal-derived foods contain all of those amino acids, while plants are typically stronger in some acids than others. Complete proteins can be made in an all vegan diet by eating a sufficient variety of foods and by getting enough calories. It was once thought that in order to get the complete proteins vegans needed to do protein combining by getting all amino acids in the same meal (the most common example is eating beans with rice) but nutritionists now know that the benefits of protein combining can be achieved over the longer period of the day. Ovo-lacto vegetarians usually do not have this problem, since egg's white and cow's milk contain all essential amino acids. Peanuts, soy milk, nuts, seeds, green peas, Legumes, the alga spirulina and some grains are some of the richest sources of plant protein.
Different foods contain different ratios of the essential amino acids. By mixing foods that are rich in some amino acids with foods that are rich in others, one can acquire all the needed amino acids in sufficient quantities. Omnivores typically eat a sufficient variety of foods that this is not an issue, however, vegetarians and especially vegans should be careful to eat appropriate combinations of foods (e.g. nuts and green vegetables) so as to get all the essential amino acids in sufficient quantities that the body may produce all the proteins that it needs.
Proteins can often figure in allergies and allergic reactions to certain foods. This is because the structure of each form of protein is slightly different, and some may trigger a response from the immune system while others are perfectly safe. Many people are allergic to casein, the protein in milk; gluten, the protein in wheat and other grains; the particular proteins found in peanuts; or those in shellfish or other seafoods. It is extremely unusual for the same person to adversely react to more than two different types of proteins.
GFI Asia Pacific is focused on advancing alternative proteins in the most populous area of the world, where both food production for export and scientific and agricultural innovation are growing rapidly.
Modifying the properties of proteins by site-directed fusion or network formation is of great significance for applications in many fields such as food processing, leather and textile fabrication, tissue engineering as well as biochemical and biomedical research. The generation of covalent bonds between proteins can be induced physicochemically by application of heat, alkaline conditions, mechanical agitation, or photooxidative treatment (Gerrard 2002; Singh 1991) by addition of chemical crosslinkers or by enzyme catalysis. Chemical crosslinking methodologies take advantage of the enormous diversity of available crosslinking reagents that differ in chemical functionality, reactivity, and size (Wong and Jameson 2012). Homobifunctional and heterobifunctional chemical crosslinkers carry two reactive groups to target proteins at the same or at different functional groups, respectively. Among these, glutaraldehyde probably represents the most commonly used crosslinking reagent (Migneault et al. 2004). Additionally, there are a few examples of multifunctional crosslinkers that can be used to target proteins at more than two functional groups simultaneously. Protein crosslinking with bi- and multifunctional crosslinkers leads to the incorporation of molecular spacer groups of defined length and composition between the reaction partners. By contrast, monofunctional crosslinkers (e.g., formaldehyde) react such that with the exception of the reactive moiety no additional linker is introduced into the final product. Furthermore, activating agents such as carbodiimides are widely used to directly connect proteins without incorporating a spacer (Wong and Jameson 2012). 59ce067264
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