Protein quality of a small mammal prey and its body organs for felids.

This study evaluated the protein quality of small mammalian prey and its body organs by analyzing amino acid (AA) composition and digestibility of wild adult rats and their body organs (skin/fur, bone, muscle, intestine, liver, kidney, spleen, brain, heart, and lung) utilizing an in vitro digestion method. The average dry matter (DM) digestibility of whole rats was 89.9%. The digestibility of total AA (TAA), total indispensable AA (TIAA), and total dispensable AA (TDAA) in whole rats was 85.6, 87.0, and 87.6%, respectively. Differences in DM digestibility were observed among rat organs, ranging from 59.0% in bone to 99.8% in muscle (P < 0.001). Highly digestible organs generally exhibited AA digestibility exceeding 90%, except for cysteine (Cys) in the intestine and kidney (83.8% and 88.9%, respectively). The digestibility of AAs in skin/fur ranged from 19.7% for Cys to 81.0% for glycine (Gly). In bone, the digestibility spanned from 56.9% for Gly to 81.1% for tyrosine (Tyr). Additionally, examining the digestible indispensable AA score (DIAAS) gives us an idea of the protein quality of small mammalian prey and their body organs. Our results complement information on AA supply and digestion during prey ingestion by felids.

As obligate carnivores, free-ranging felids consume prey and rely on nutrients from animal organs. Studies in adult carnivores such as domestic cats have demonstrated the importance of the dietary amino acid profile. Therefore, this research used rats as a small prey model to analyze the amino acid composition and digestibility of whole prey and its body organs through in vitro digestion methods. Our results add information on amino acid supply and digestion during natural food intake in felids.

Beyond the Bowl: Understanding Amino Acid Requirements and Digestibility to Improve Protein Quality Metrics for Dog and Cat Foods.

The determination of amino acid (AA) requirements for mammals has traditionally been done through nitrogen (N) balance studies, but this technique underestimates AA requirements in adult animals. There has been a shift toward researchers using the indicator amino acid oxidation (IAAO) technique for the determination of AA requirements in humans, and recently in dogs. However, the determination of AA requirements specific to adult dogs and cats at maintenance is lacking and the current requirements outlined by the National Research Council are based on a dearth of data and are likely underreporting the requirements of indispensable AA (IAA) for the population. To ensure the physiological requirements of our cats and dogs are met, we need methods to accurately and precisely measure digestibility. In vivo methods, such as ileal cannulation, are most commonly used, however, due to ethical considerations, we are moving away from animal models and toward in vitro methods. Harmonized static digestion models have the potential to replace in vivo methods but work needs to be done to have these methods more accurately represent the gastrointestinal tract (GIT) of cats and dogs. The Digestible IAA Score (DIAAS) is one metric that can help define protein quality for individual ingredients or mixed diets that uses AA SID estimates and ideally those can be replaced with in vitro AA digestibility estimates. Finally, we need accurate and reliable laboratory AA analyses to measure the AA present in complete diets, especially those used to quantify methionine (Met) and cysteine (Cys), both often limiting AAs in cat and dog diets. Together, this will guide accurate feed formulation for our companion animals to satisfy requirements while avoiding over-supplying protein, which inevitably contributes to excess N excretion, affecting both the environment and feed sustainability.

In vitro digestibility and solubility of phosphorus of three plant-based meat analogues.

Interest in plant-based meat analogues has increased and can be expected to be applied to pet foods, which necessitates the understanding of the nutrient supply in those foods. Our primary aim was to advance our understanding of the digestive properties of sterilized plant-based meat analogues. The impact of the preparatory processing steps on the solubility of meat analogues was studied. Meat analogues were made by mixing water, salt, and wheat gluten with soy protein isolate, pea protein isolate, or faba bean concentrate. Mixed materials were processed into model meat analogues using shear cell technology. Products were canned in water or gravy and sterilized. An animal-based canned pet food was made as a reference. Products sampled at the processing steps (mixing, shearing, sterilization) were digested in vitro. Samples of digestate were taken at the gastric phase (0 and 120 min) and small intestinal phase (120, 200, 280, and 360 min) for analysis of protein hydrolysis. The extent digestion of nitrogen and dry matter was determined at the end of incubation. Total phosphorus, soluble phosphorus after acid treatment, and after acid and enzymatic treatment were determined. The degree of hydrolysis after gastric digestion was low but increased immediately in the small intestinal phase; products based on pea had the highest values (56%). Nitrogen digestibility was above 90% for all materials at each processing step, indicating that bioactive compounds were absent or inactivated in the protein isolates and concentrate. Phytate seemed to play a minor role in meat analogues, but phosphorus solubility was influenced by processing. Shearing decreased soluble phosphorus, but this effect was partly reversed by sterilization. Nutrient digestibility as well as phosphorus solubility in plant-based products was higher than or comparable with the reference pet food. These findings show that the digestive properties of the tested plant-based meat analogues do not limit the supply of amino acids and phosphorus.