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Kinetics of peptides generated during static INFOFEST in vitro digestion of mealworms and crickets compared to chicken breast

ABSTRACT: Mealworms and crickets are edible protein-dense insects that can be produced more sustainably than animal proteins from livestock, and are therefore promising alternative protein sources for human consumption. The protein amount provided by a food source is, however, dependent on the protein digestibility. To evaluate hydrolysis of insect proteins compared to the highly digestible chicken breast, mealworms and crickets that underwent different food preparation and processing steps (blanching, oven-drying, freeze-drying and dechitinization) were subjected to the static INFOGEST in vitro digestion protocol. Peptide patterns were created by sampling in vitro digesta multiple times throughout the in vitro digestion protocol (one sample in the oral phase, and ten in the gastric as well as the intestinal phase). Peptides in digesta were isolated, and samples from the different time points were measured by LC-MS analysis.

INSTRUMENT(S): LTQ

ORGANISM(S): Gallus Gallus (chicken) Tenebrio Molitor Acheta Domesticus

TISSUE(S): Whole Body

SUBMITTER: Reto Portmann

LAB HEAD: Reto Portmann

PROVIDER: PXD041373 | Pride | 2023-06-23

REPOSITORIES: pride

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Project description:Germination offers advantages to improve legume protein digestibility as it disintegrates seed structure and hydrolyzes proteins and anti-nutrients. Seed permeability (related to polyphenol content of seed coats) is an important factor affecting the duration of seed germination and its impact in protein digestibility and bioactivity. The objective was to compare the effect of seed germination on protease activity, structure and proteolysis of four selected legumes with contrasting seed coat polyphenol profiles (gray zero tannin [GZL], beluga [BL] and dehulled red [DL] lentils; and zero tannin/low vicine-convicine fava bean [ZF]). Protein hydrolysis was characterized during germination and digestion with respect to proteins, peptides and free amino acids (FAA). In vitro antihypertensive and antioxidant activities of digests were investigated, and peptidomic characterization (HPLC-MS/MS) and identification of bioactive fragments in intestinal digests were performed. Regardless of seed type, germination increased protease activity and reduced levels of phytic acid, trypsin inhibitors and tannins (only in BL). Significant proteolysis of the 7S and 11S globulins and concomitant increase peptides and FAA was observed in all sprouted legumes. Digestion kinetics in sprouts revealed a faster generation of FAA and peptides than in dry seeds, with changes more evident for DL associated to faster imbibition, germination and sprout growth. In contrast, BL sprouts showed the lowest protein digestibility, likely due to lower protease activity levels, seed structure disintegration and higher anti-nutrient levels in comparison to GZL, DL and ZF. Moreover, digestion of sprouts resulted in a higher number of resistant peptides in DL and ZF that matched with previously reported bioactive sequences, suggesting a promising health potential of legume sprouts that was confirmed in vitro. Results suggested that the germination process improved protein digestibility and health promoting potential of lentil and fava bean proteins although these changes were more evident in DL due to its rapid imbibition, faster germination and sprout development. This study will provide important information for either plant breeders to develop legume varieties with permeable seed coats or food producers that could use dehulled seeds for efficient production of sprouts as sustainable food sources of plant proteins with improved nutritional and healthy properties.

			Action	DRS
	ADfd_01_SSF.dat	Other
	ADfd_02_SGF0.dat	Other
	ADfd_03_SGF0.5.dat	Other
	ADfd_04_SGF1.dat	Other
	ADfd_05_SGF3.dat	Other

Dataset Information

Kinetics of peptides generated during static INFOFEST in vitro digestion of mealworms and crickets compared to chicken breast

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