Microencapsulation Essay

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Nowadays, there is great interest in the development of functional foods and beverages containing lipophilic bioactive agents that exhibit health benefits, such as oil-soluble vitamins and nutraceuticals. Microencapsulation has been utilized as a technique for the fortification and controlled release of functional food components such as antioxidants, flavors, fatty acids, vitamins, minerals, and so on (Estevinho and others 2013; Aguiar and others 2016; Gonçalves and others 2016, 2018). A number of microencapsulation techniques for bioactive compounds such as functional edible oils are applied which can be generally divided into 2 separate categories physical (for example, spray-drying) and chemical (for example, complex coacervation) techniques …show more content…

These functional fatty acids have an effective role in treatment/prevention a high number of diseases or disorders such as cognitive decline, Alzheimer's disease, arthritis pains, gastrointestinal cancer, and heart and cardiovascular diseases (Lecerf 2009; Gharibzahedi and others 2013a, 2013b, 2014; Abdulrazaq and others 2017; Cederholm 2017; Eltweri and others 2017; Saljoughian and others 2017). Microencapsulation protects products containing relatively high amounts of ω-3/ω-6 unsaturated fatty acids from oxidation reactions during the exposure to oxygen, metal-ions, light, and high temperatures that leads to oxidative rancidity, polymerization, and color changes. Hence, application of this technology helps in protecting the organoleptic qualities of fatty food and ensures the delivery of bioactive agents in the gut (Gharibzahedi and others 2013a, 2013b; Pourashouri and others 2014a, 2014b; Xia and others 2017). Thus, inclusion of lipophilic components into a polymeric matrix can improve their bioavailability/bioaccessibility through the prevention or reduction of unwanted interactions between PUFAs and other food ingredients (Timilsena and others 2016a; …show more content…

TGase or glutaminyl-peptide-amine γ-glutamyl transferase (EC 2.3.2.13) is able to create covalent crosslinks of inter- or intramolecular ε-(γ-glutamine)-lysine isopeptidic bonds through catalysis of the acyl transfer reaction from a γ-carboxyamide group in protein-bound glutamine residues (acyl donor) to a ε-amino group in a protein-bound lysine residue (acyl acceptor) (Figure 1). This crosslinking reaction can lead to the formation of protein polymers with high molecular weight (DeJong and Koppelman 2002; Gharibzahedi and others 2018). Cross-linking of available functional groups of proteins by TGase also provides the possibility of tuning protein functional characteristics such as, solubility, water holding capacity, gelation, thickening, emulsification, and heat stability (Gharibzahedi and Jafari 2017a, 2017b, 2017c). Moreover, this crosslinking enzyme can easily be produced from microorganisms particularly Streptomyces mobaraensis in a fermentation system (Gan and others 2008). TGase exhibits activity in the pH range from 5 to 8, with a maximum around pH 7. In addition, it has been shown to maintain its activity up to 50 °C, but be inactivated at higher temperatures (Kieliszek and Misiewicz 2014). TGase can be a powerful tool to crosslink proteins in wall materials of PUFAs-loaded microcapsules owing to the cost-effective

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