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In: Book of Abstracts of the 65th Annual Meeting of the European Association for Animal Production
In: Book of Abstracts of the 65th Annual Meeting of the European Association for Animal Production

Insects, a staple feed for wild birds and free ranging poultry, have a relatively high protein quality and are a promising feed for commercial poultry. Replacing soybean meal with insect derived feeds potentially reduces dependency on feed imports, increasing the sustainability of egg production – but only if maintaining or enhancing their nutritional quality. This study investigated egg fatty acid (FA) profiles from replacing soyabean meal withHermetia illucens (black soldier fly) meal (HIM) for laying hens. A three-week trial with 30 organic Lohman Selected Leghorn hens between 64-74 weeks old was repeated with four flocks at the end of their first laying cycle. In all replicate trials, ten birds were randomly allocated to each of three diets: (1) control with 360 g soybean/kg and no HIM; (2) H12 with 120 g HIM and 156 g soybean/kg; and (3) H24 with 240 g HIM/kg and no soybean. Complete replacement of soya (H24) increased saturated fatty acid (SFA) and monounsaturated fatty acids (MUFA) and decreased total polyunsaturated fatty acids (PUFA), omega-6 (n-6) and omega-3 (n-3) PUFA concentrations in eggs. The intermediate H12 diet (replacing 33% soya) gave similar n-3 and MUFA concentrations to control eggs but significantly increased SFA and reduced total PUFA. However, birds moderated the transfer of high intakes of potentially damaging C12:0 and C14:0 into eggs and although differences in eggs were highly significant and great (relative to very low levels in control eggs) concentrations were substantially lower than in insect meal itself and some commonly consumed foods.

Open Access
In: Journal of Insects as Food and Feed

Abstract

Unsustainable agriculture contributes to disastrous global effects – insect-based feed shows potential due to their sustainable, nutritional, and waste upcycling properties. Current EU legislation restricts insect-based meals to fish, pork, and poultry feed; but the near-future shows a great potential for wider acceptance in livestock feed. Black soldier fly larvae (BSFL), mealworm (MW), field cricket (FC), and banded cricket (BC) were sourced within three consecutive weeks – each batch was prepared, freeze-dried, then milled, and stored at −20 °C. Chemical composition of whole-insect meals was analysed for ether extract (EE), crude ash, and nitrogenic contents using standard wet chemistry protocols. Monogastric in vitro digestibility was determined through replicating gastric and full intestinal digestion; during this, R-amino acid content was determined through protein hydrolysis kinetics. Additionally, ATR-FTIR was used for molecular analysis, including identification of nutrient-associated functional spectral bands – structural differences were compared through principal component analysis. Insect-based ATR-FTIR analysis demonstrates notable differences in Amide regions, suggesting distinct protein secondary structures, but overall, FC and BC contain the highest crude protein (CP) levels. The lowest CP content was in BSFL; however, BSFL contained the highest ash content – likely consequence of high calcium. Dry matter (DM) yielded lowest in the crickets (FC-28.6; BC-26.9 g/100 g), and highest in MW-38.5 g/100 g; the sum of CP + EE in MW represented >80% DM, but with higher EE contents-CP: EE = 2.45. Data shows greater chitin content in crickets than BSFL + MW. Crickets showed greater neutral detergent fibre (NDF) than BSFL + MW; however, acid-detergent fibre (ADF) was similar among all species, suggesting NDF may include amalgams of interlinked nutrients released by acid digestion. This first study shows for the first time evidence that rearing conditions and substrates influences molecular structure. Exponential solubilisation was observed during pepsin + pancreatin digestion for all, but BSFL exhibited the highest degree-of-hydrolysis during the pancreatin phase, surpassing others. Analysis indicates protein hydrolysis differences are linked to trypsin activity susceptibility.

Open Access
In: Journal of Insects as Food and Feed