Justyna Borawska

Background/Objectives: The nutrition and lifestyle choices made during pregnancy significantly impact the long-term health of both mother and child. This observational study, conducted at the Jersey Maternity Unit, investigated how maternal diet and weight influence delivery outcomes and newborn feeding methods among 81 pregnant women. The aim of the study was to assess whether maternal diet, weight changes, and infant feeding practices vary according to ethnicity and duration of residence in Jersey, in order to inform culturally sensitive health improvement strategies. Methods: The FFQ was used to characterise the diet before and during pregnancy. Diet quality was assessed by the 9-item aMED score. Data on anthropometric measurements (including gestational weight gain, GWG), socioeconomic characteristics, and infant feeding methods (including breastfeeding rates) were collected. Results: The statistical analyses evaluate differences and distribution of data in the groups of women based on the ethnicity and period the mothers had lived on the island. For all the women, there were significant changes in the weight gained at week 28 compared to weeks 8 and 12 (+8.0 (4.0; 12.1) kg, p ≤ 0.001), as well as the period before pregnancy until the 34th week of gestation (+11.9 (8.0; 12.1) kg, p ≤ 0.001). The intake of low-fat dairy, whole grains, and fruit changed through the gestation period and differed between pregnant women with different periods of island residence. There were no changes in the aMED score and adherence. Conclusions: Maternal weight gain followed a consistent pattern during pregnancy, whereas dietary behaviours—particularly the consumption of key food groups—varied by cultural background and length of residence. These findings emphasise the need for culturally sensitive antenatal care and tailored nutrition strategies to improve maternal outcomes, support breastfeeding, and reduce long-term health risks for mothers and children in Jersey’s multicultural population.

Bovine milk protein preparations (MPPs), namely micellar casein concentrate (MCC), serum protein concentrate (SPC), and MCC with ultrafiltrated buttermilk permeate (MBP), were analyzed as sources of inhibitors of angiotensin-converting enzyme (i.e., ACE) and dipeptidylpeptidase IV (i.e., DPP-IV) as well as antioxidative peptides. The studies involved in silico predictions of the release of biopeptides from bovine milk proteins. Then, all MPPs were subjected to the simulated gastrointestinal digestion using the INFOGEST protocol. Results using a BIOPEP-UWM database tool indicated that 59 biopeptides exhibiting the above-mentioned activities could be produced upon the action of pepsin, trypsin, and chymotrypsin. Thirty-six biopeptides were identified in at least one of the three MPPs subjected to the INFOGEST protocol. MCC before simulated digestion exhibited the strongest ACE-inhibiting activity among all MPPs (IC₅₀ = 1.856 mg/mL). The weakest ACE inhibitory effect was demonstrated for MBP after duodenal digestion (i.e., MBP D; IC₅₀ = 7.627 mg/mL). The above MPP showed the strongest DPP-IV-inhibiting activity (IC₅₀ = 0.0067 mg/mL). All MPPs exhibited antioxidative activity, with the strongest ABTS^•+ (i.e., 2,2′-azino-bis(3-ethylbenzotialozline-6-sulfonic acid) radical scavenging effect shown for MBP D (IC₅₀ = 2.754 mg/mL), and the strongest DPPH^• (i.e., 2,2-diphenyl-β-picrylhydrazyl) radical scavenging activity (IC₅₀ = 1.238 mg/mL) demonstrated for SPC D. Among all MPPs, SPC D also exhibited the highest FRAP (i.e., Ferric Reducing Antioxidant Power) bioactivity (IC₅₀ = 13.720 mg/mL), whereas MBP D was the MPP with the lowest FRAP potential (IC₅₀ = 20.140 mg/mL). The present study results show the potential of all MPPs as functional additives to support health-beneficial functions of dairy products.

The aim of this study was to characterize the digests and peptides derived from oat kernel proteins in terms of their major enzyme inhibitory activities related to the prevention of cardiometabolic syndrome. It also entailed the characteristics of antioxidant bioactivity of the analyzed material. The study was carried out using coupled in silico and in vitro methods. The additional goal was to investigate whether identified peptides can pervade Caco-2 cells. Based on the results of bioinformatic analysis, it was found that the selected oat proteins may be a potential source of 107 peptides with DPP-IV and/or ACE inhibitory and/or antioxidant activity. The duodenal digest of oat kernels revealed multiple activities. It inhibited the activities of the following enzymes: DPP-IV (IC₅₀ = 0.51 vs. 10.82 mg/mL of the intact protein), α-glucosidase (IC₅₀ = 1.55 vs. 25.20 mg/mL), and ACE (IC₅₀ = 0.82 vs. 34.52 mg/mL). The DPPH^• scavenging activity was 35.7% vs. 7.93% that of the intact protein. After in silico digestion of oat proteins, 24 peptides were selected for identification using LC-Q-TOF-MS/MS. Among them, 13 sequences were successfully identified. One of them, i.e., VW peptide, exhibited triple activities, i.e., DPP-IV and ACE inhibitory and DPPH^• scavenging activity. The multifunctional peptides: PW, TF, VF, and VW, were identified in the basolateral samples after transport experiments. Both in silico and in vitro analyses demonstrated that oat kernel proteins were the abundant sources of bioactive digests and peptides to be used in a diet for patients suffering from cardiometabolic syndrome.

Apart from the classical (experimental) methods, biologically active peptides can be studied via bioinformatics approach, also known as in silico analysis. This study aimed to verify the following research hypothesis: ACE inhibitors and antioxidant peptides can be released from salmon and carp proteins during simulated in silico human-like gastrointestinal digestion. The potential to release biopeptides was evaluated using the BIOPEP-UWM quantitative criteria including the profile of biological activity, frequency of the occurrence (A)/release (A_E) of fragments with an ACE inhibitory or antioxidant activity by selected enzymes, and relative frequency of release of bioactive fragments with a given activity by selected enzymes (W). Salmon collagen and myofibrillar proteins of carp turned out to be the best potential source of the searched peptides–ACE inhibitors and antioxidant peptides. Nonetheless, after digestion, the highest numbers of ACE inhibitors and antioxidant peptides were potentially released from the myofibrillar proteins of salmon and carp. Peptide Ranker Score, Pepsite2, and ADMETlab platform were applied to evaluate peptides’ bioactivity potential, their safety and drug-like properties. Among the 63 sequences obtained after the simulated digestion of salmon and carp proteins, 30 were considered potential biopeptides. The amino acid sequences of ACE-inhibiting and antioxidant peptides were predominated by P, G, F, W, R, and L. The predicted high probability of absorption of most analyzed peptides and their low toxicity should be considered as their advantage.

Carp muscle tissue is a valuable source of biologically active constituents known to positively influence human health. In this study, carp protein digests/hydrolysates generated by human/porcine digestive enzymes were analysed for their angiotensin I-converting enzyme inhibitory (ACEi) activity. The ex vivo digests and in vitro hydrolysates were used in a screening for ACEi peptides as well. Carp proteins were hydrolysed more rapidly by human gastrointestinal juices than by porcine enzymes. Sarcoplasmic protein fractions were digested/hydrolysed more easily than the myofibrillar ones. The inhibitory concentrations at 50% (IC50) for ex vivo digested sarcoplasmic and myofibrillar protein fractions were established at 1.50 and 1.04 mg/mL, respectively. While, for in vitro hydrolysed sarcoplasmic and myofibrillar protein fractions, the IC50 values were calculated as 2.57 and 1.12 mg/mL, respectively. The digested/hydrolysed samples of carp sarcoplasmic and myofibrillar protein fractions were separated by RP-HPLC-MS Amino acid sequences were identified with the use of the LC-MS/MS method coupled with in silico systematic screening for ACEi pep tides. ACEi peptides with IVY, IY, VY, ALPHA and VKAGF sequences were found in the carp digests/hydrolysates. In the ex vivo carp digest, an ACEi peptide TVY was also detected, while the ACEi peptide IW was identified in in vitro hydrolysate. Our study showed that different ACEi effects of carp digests and hydrolysates were generated with the use of human gastrointestinal and porcine enzymes.

Open Access Agricultural Journals published by Institute of Agricultural Economics and Information

BACKGROUND: Salmon (Salmo salar L.) myofibryllar protein (MP) and sarcoplasmic protein (SP) were digested with human gastric and duodenal juices and hydrolysed in vitro with commercial pepsin and Corolase PP.RESULTS: The digestion after duodenal juice/Corolase PP caused almost complete breakdown of peptide bonds in MP and SP. The DPPH^• scavenging activity of proteins decreased during both ex vivo digestion and in vitro hydrolysis. The highest value of DPPH^• scavenging activity was shown for the gastric digest of SP (8.88 ± 0.87%). The ABTS^+• scavenging activity of MP and SP increased during digestion/hydrolysis. The duodenal digest of SP was characterised by the highest value of ABTS^+• scavenging activity (72.7 ± 1.2%). In turn, the highest value of ferric‐reducing power was determined for the gastric digest of SP (84.8 ± 0.2%). Salmon antioxidant peptides Phe‐Ile‐Lys‐Lys, His‐Leu, Ile‐Tyr, Pro‐His‐Leu, Pro‐Trp, Val‐Pro‐Trp were identified in both ex vivo digested and in vitro hydrolysed MP and SP. An antioxidant peptide, Val‐Tyr, was additionally detected in the in vitro hydrolysate of SP.CONCLUSION: The results indicate the salmon myofibrillar and sarcoplasmic protein fractions as potential sources of antioxidant peptides that could be released in the gastrointestinal tract but their amino acid sequence and quantification vary. © 2015 Society of Chemical Industry