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      A novel meat quality improver composed of carrageenan and superfine smashed okra powder and its application in chicken meatballs

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          Abstract

          The study investigated the effects of the addition of 0% (control group, CG), 0.25, 0.35, and 0.45% superfine smashed okra powder (SSOP) or carrageenan (CAR), and 0.25% SSOP – 0.35% CAR complex (OC) on the quality of chicken meatballs. Chicken meatballs fabricated with the SSOP-CAR complex showed better quality as compared to the other treatments. The lowest cooking loss was observed in the OC group, which corresponded to significantly decreased relaxation times of low-field nuclear magnetic resonance (LF-NMR) ( T 21 and T 22) ( P < 0.05). Compared to CG, The L* and a* values of chicken meatballs were significantly decreased due to the addition of SSOP ( P < 0.05), and the additions of SSOP and CAR significantly increased the storage modulus ( G′) and loss modulus of chicken meat batter upon heating ( P < 0.05). Besides, the OC and 0.45% CAR groups showed the highest texture profile values for hardness and chewiness ( P < 0.05). The sensory evaluation revealed that the chicken meatballs emulsified with the OC had the best overall acceptability. The results indicated that OC could be a great feasible and potential application in the meat industry, especially in the development of functional emulsified meat products.

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          Most cited references38

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          Molecular forces involved in heat-induced pea protein gelation: Effects of various reagents on the rheological properties of salt-extracted pea protein gels

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            Rheological and microstructural properties of porcine myofibrillar protein-lipid emulsion composite gels.

            The objective of the study was to investigate the role of emulsified fat (lard) and oil (peanut oil) in the rheology and microstructure of porcine myofibrillar protein (MP) gels. Heat-induced composite gels were prepared from 2% MP with 0% to 15% pre-emulsified lipids at 0.6 M NaCl, pH 6.2. Dynamic rheological testing upon temperature sweeping (20 to 80 degrees C at 2 degrees C/min) showed substantial increases in G' (an elastic modulus) of MP sols/gels with the addition of emulsions. Gel hardness was markedly enhanced (P or=10% emulsions, and the composite gel with 15% lard was 33% more rigid (P < 0.05) than that with 15% peanut oil. Incorporation of both emulsions at 10% or higher levels improved the water holding capacity of the gels by 28% to 44% (P < 0.05). Light microscopy revealed a compact gel structure filled with protein-coated fat/oil globules that interacted with the protein matrix via disulfide bonds. The results indicated that both physical and chemical forces contributed to the enhancements in the rheology, moisture retention, and lipid stabilization in the MP-emulsion composite gels.
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              Hydroxyl radical and ferryl-generating systems promote gel network formation of myofibrillar protein.

              The objective of the study was to examine how oxidatively induced protein cross-linking would influence the gelation properties of myofibrillar protein (MP) under meat processing conditions. MP suspensions in 0.6 M NaCl at pH 6 were treated with an iron-catalyzed oxidizing system (IOS: 10 microM FeCl(3), 0.1 mM ascorbic acid, 0.05 to 5 mM H(2)O(2)) or a H(2)O(2)-activated metmyoglobin oxidizing system (MOS: 0.01 to 0.1 mM metmyoglobin/H(2)O(2)) that produced hydroxyl radical and ferryl species, respectively. Both oxidizing systems promoted MP thermal gelation, which was evidenced by rapid protein-protein interaction and the enhancement in storage modulus (elasticity) of the gel network as revealed by dynamic rheological testing in the 20 to 74 degrees C temperature range. This gelation-enhancing effect was attributed to the shift of myosin aggregation in the early stage of heating from predominantly head-head association (nonoxidized control samples) to prevalently tail-tail cross-linking through disulfide bonds. However, both hardness and water-holding capacity of chilled gels tended to decline when MP was exposed to >or=1 mM H(2)O(2) in IOS and to all concentrations of metmyoglobin in MOS. Microscopic examination confirmed a more porous structure in oxidized gels when compared with nonoxidized protein gels. The results demonstrated that mild oxidation altered the mode of myosin aggregation in favor of an elastic gel network formation, but it did not improve or had a negative effect on water-binding properties of MP gels.
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                Author and article information

                Journal
                International Journal of Food Engineering
                Walter de Gruyter GmbH
                1556-3758
                2194-5764
                May 24 2021
                March 25 2021
                May 01 2021
                May 24 2021
                March 25 2021
                May 01 2021
                : 17
                : 5
                : 377-384
                Affiliations
                [1 ]College of Food Engineering , Anhui Science and Technology University , Fengyang 233100 , China
                [2 ]Anhui Engineering Laboratory for Agro-products Processing , Anhui Agricultural University , Hefei 230036 , P. R. China
                Article
                10.1515/ijfe-2020-0299
                dbb61d0d-4d9e-440e-995f-0fd307a6eb36
                © 2021
                History

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