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Effect of HHP, Enzymes and Gelatin on Physicochemical Factors of Gels Made by Using Protein Isolated from Common Cricket (Acheta domesticus).

ABSTRACT: The effect of high hydrostatic pressure (HHP) combined with enzymatic methods or gelatin incorporation in the gelation process of protein isolated from Acheta domesticus was investigated. The results indicate that transglutaminase (TGasa) or glucose oxidase (GOx) enzymes can induce reversible aggregation in dispersions of insoluble protein fractions and increase viscosity in dispersions of soluble fractions, but does not induce gel formation even after HHP treatment; in consequence, enzymatic treatment on cricket protein can be used to increase viscosity but not to form gels. It is technically feasible to obtain gels by adding 2% porcine gelatin to dispersions of protein fractions and subjecting them to HHP. The firmness and syneresis variation values of those gels during storage depended on the protein extracted fraction (insoluble or soluble protein) and on the concentration of protein used. The highest hardness and lowest syneresis was found with the gels obtained from the insoluble fraction at 11 and 15% (w/w) protein concentration. Color difference (ΔE* > 3) appreciable to the naked eye was observed along the storage period and no noticeable pH variations were found after 28 days of storage. Results indicate that new raw materials of interest can be developed for the food industry based on cricket protein isolates, to make high-protein foods which could be applied in a wide variety of different food applications including 3D printing or fat substitution.

SUBMITTER: Urbina P

PROVIDER: S-EPMC8071182 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:The newly laid eggs of the house cricket Acheta domesticus contain apolar ecdysteroid conjugates, which we have hypothesized to be ecdysone long-chain fatty acyl esters [Whiting & Dinan (1988) J. Insect Physiol., in the press]. The ovaries of mature adult female A. domesticus in vitro convert [3H]ecdysone into apolar conjugates identical with those found in newly laid eggs. Comparison of the radioactive metabolites produced on incubation of [3H]ecdysone with various organs of adult female A. domesticus in vitro indicate that the fat-body is the major producer of polar ecdysteroid metabolites at this stage of development, whereas the ovaries are the major site of production of apolar metabolites. Apolar metabolites are also produced to a lesser extent by the crop, gut sections and the fat-body. Hydrolysis of radioactive metabolites produced by the ovaries with Helix enzymes releases only [3H]ecdysone, and thus ecdysone is not metabolized before conjugation by the ovaries. Formation of chemical derivatives (acetonide and acetates) of these 3H-labelled apolar conjugates strongly indicates that the position of conjugation is through the hydroxy group at C-22 of ecdysone. Extensive chromatographic analysis of the 3H-labelled apolar metabolites produced by the ovaries by t.l.c. and h.p.l.c. and comparison with authenticated reference compounds have conclusively demonstrated that the conjugates consist of ecdysone esterified at C-22 to a mixture of common long-chain fatty acids. The major fatty acyl esters have been identified and their percentage contribution to the mixture determined: laurate (0.5%), myristate (2.8%), palmitate (25.8%), stearate (8.4%), arachidate (1.0%), oleate (15.7%), linoleate (38.8%) and linolenate (2.1%). In addition there are three minor unidentified peaks, one of which has been tentatively identified as ecdysone 22-palmitoleate (2.6%). Comparison of this percentage composition with the previously published fatty acid composition of A. domesticus haemolymph [Wang & Patton (1969) J. Insect Physiol. 15, 851-860] reveals remarkable similarities, indicating that the acyl transferase(s) forming the conjugates have a broad specificity with regard to the fatty acyl substrate.

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Effect of HHP, Enzymes and Gelatin on Physicochemical Factors of Gels Made by Using Protein Isolated from Common Cricket (Acheta domesticus).

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