This experiment aimed to evaluate the impact of dietary hydroxyproline (Hyp) supplementation on the muscle quality of juvenile Pacific white shrimp (Litopenaeus vannamei) fed a low fishmeal diet. Six formulated diets included one high fishmeal (HF; 25% fishmeal content) and five low fishmeal diets (10% fishmeal content) with 0%, 0.2%, 0.4%, 0.6% and 0.8% Hyp (LF0, LF2, LF4, LF6 and LF8, respectively). Each diet was assigned to four replicates, and 40 shrimp (0.32 ± 0.00 g) per replicate were fed four times a day for 8 weeks. Dietary Hyp supplementation had little effects on growth performance, but increased the contents of Hyp, prolyl 4-hydroxylases (P4Hs), and collagen. The meat yield, springiness, hardness, chewiness, and cohesiveness of muscle were the highest in the LF4 group among the low fishmeal groups (P < 0.05). Cooking loss and freezing loss of muscle were the lowest in the LF4 group (P < 0.05). Dietary supplementation with 0.4% Hyp increased the myofiber density and decreased the myofiber diameter of muscle (P < 0.05). Supplementation of Hyp in the diet up-regulated the mRNA expression of smyhc5, smyhc15, col1a1, col1a2, igf-1f, tgf-β and tor and down-regulated the mRNA expression of smyhc1, smyhc2, smyhc6a (P < 0.05). Supplementation of Hyp in the diet up-regulated the protein expression of P-4E-BP1, P-AKT, AKT and P-AKT/AKT (P < 0.05). These results suggested that the addition of 0.4% Hyp to low fishmeal diets improved the muscle quality of L. vannamei.

The current feeding study was designed to validate the two dietary essential amino acid profiles (EAAP) established based on linear broken-line (LBL) and quadratic broken-line (QBL) models, in a previous study, against Evonik (AMINOHen) and breeder recommendations for ISA Brown layers for peak production (PP, 20 to 44 weeks of age), and post peak production (post PP, 44 to 75 weeks of age). The EAAP based on LBL models on average had 19.5% and 26.0% lower digestible AA (Lys, Met + Cys, Thr, Trp, Ile and Val), than the EAAP based on QBL models for PP and post PP, respectively. The EAAP based on AMINOHen and breeder recommendation had lower digestible AA than QBL, and higher EAAP than LBL models for both production phases. At 20 weeks of age, 224 ISA Brown layer hens were weighed and randomly allocated to individual battery cages. Each of the four diets was replicated 8 times with 7 birds per replicate. Egg production was recorded daily, and egg weights were measured at the end of each week. Feed consumption was measured at the end of each period. The egg production rate was not significantly affected by the diets and remained at around 98.0% (PP) and 95.0% (post PP) (P > 0.05). Birds fed diets based on LBL recommendation consistently laid smaller eggs, resulting in a lower egg mass (59.8 vs. 62.0 g egg/hen per day during PP, and 60.3 vs. 63.0 g egg/hen per day during post PP; P < 0.05). Diets had no significant effect on feed intake and body weight (P > 0.05). The highest feed conversion ratio (FCR) during PP (P = 0.067) and post PP (P < 0.05) was recorded for the birds offered diets based on LBL recommendation. In conclusion, all four EAAP tested in this study support an above average egg production rate. However, the EAAP based on LBL models may potentially decrease the input feed cost per kilogram of eggs but are not set to optimise FCR and maximise egg mass.

Phytin is the Ca2+-Mg2+-K+ salt of phytic acid that is created and deposited in the aleurone layer and/or germ of grains and legumes. Its high presence in feedstuffs for fowl and swine diets results in it being a universal and significant impediment to optimum performance. Phytin impairs gastrointestinal recovery of a wide array of nutrients, the effect varying with the nutrient concerned. On exposure to low pH during gastric digestion, phytin dissociates into phytic acid and solubilized Ca2+. Even at low gastric pH, phytic acid is negatively charged which forms the basis of its anti-nutritive behavior. Pepsinogen has extensive basic amino acids on its activation peptide that are presented as cations at low pH which are targeted by pepsin for activation. Partially crystalized Ca2+ near the enzyme's active site further stabilizes its newly formed structure. Thus, phytic acid appears to interfere with gastric digestion by several mechanisms; interfering with pepsinogen activation by binding to the polypeptide's basic amino acids; coordinating free Ca2+, destabilizing pepsin; binding some dietary proteins directly, further compromising gastric proteolysis. Upon digesta attaining neutrality in the duodenum, Ca2+ and other cations re-bind with accessible anions, phytic acid being a significant contender. Phytate not only binds free cations but can also strip them from enzymes (e.g. Ca2+, Zn2+) which reduces their structural resistance to autolysis and ability as co-factors (e.g. Zn2+) to increase enzyme activity. Goblet cells initially employ Ca2+ as an electronic shield between mucin layers enabling granule formation and cell storage. After mucin granule release, Ca2+ is progressively displaced by Na+ to free the viscous mucins enabling its translocation. Mucin entangles with the glycocalyx of adjacent enterocytes thereby constructing the unstirred water layer (USWL). Excessive removal of Ca2+ from mucin by phytic acid increases its fluidity facilitating its loss from the USWL with its associated Na+. This partly explains increased mucin and Na+ losses noted with high phytate diets. This review suggests that phytic acid binding of Ca2+ and less so Zn2+ is the basis for the diversity in nutrient losses encountered and that such losses are in proportion to dietary phytate content.