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When presented with a lineup, the witness is tasked with identifying the culprit or indicating that the culprit is not present. The witness then qualifies the decision with a confidence judgment. But how do witnesses go about making these decisions and judgments? According to absolute-judgment models, witnesses determine which lineup member provides the strongest match to memory and base their identification decision and confidence judgment on the absolute strength of this MAX lineup member. Conversely, relative-judgment models propose that witnesses determine which lineup member provides the strongest match to memory and then base their identification decision and confidence judgment on the relative strength of the MAX lineup member compared to the remaining lineup members. We took a critical test approach to test the predictions of both models. As predicted by the absolute-judgment model, but contrary to the predictions of the relative-judgment model, witnesses were more likely to correctly reject low-similarity lineups than high-similarity lineups (Experiment 1), and more likely to reject biased lineups than fair lineups (Experiment 2). Likewise, witnesses rejected low-similarity lineups with greater confidence than high-similarity lineups (Experiment 1) and rejected biased lineups with greater confidence than fair lineups (Experiment 2). Only a single pattern was consistent with the relative model and inconsistent with the absolute model: suspect identifications from biased lineups were made with greater confidence than suspect identifications from fair lineups (Experiment 2). The results suggest that absolute-judgment models better predict witness decision-making than do relative-judgment models and that pure relative-judgment models are unviable., (Copyright © 2024 Elsevier B.V. All rights reserved.)

The impact of different light conditions during culture on the nitrogen, protein, colour, total phenolic content (TPC) and amino acid profile of Palmaria palmata biomass was investigated. P. palmata was cultured using different light regimes, i.e., white (1 and 2), red, blue and green over 12 days. A significant decrease ( p < 0.05) in total nitrogen (TN), non-protein nitrogen (NPN) and protein nitrogen (PN) was observed on day 6 while an increase was observed on day 12 in P. palmata samples cultured under blue light. The protein content (nitrogen conversion factor of 4.7) of the initial sample on day 0 was 15.0% ( w / w ) dw whereas a maximum protein content of 16.7% ( w / w ) was obtained during exposure to blue light following 12 days culture, corresponding to an 11.2% increase in protein content. Electrophoretic along with amino acid profile and score analyses showed light-related changes in protein composition. The lighting regime used during culture also influenced the colour parameters (lightness L*, redness a*, yellowness b* and colour difference ΔE) of milled algal biomass along with the TPC. Judicious selection of lighting regime during culture may allow the targeted production of sustainable high-quality proteins from P. palmata.

Border control officers may be on the lookout for wanted people while they verify that travellers match their passport photos. We developed a novel experimental paradigm to investigate whether people are more likely to report that someone is wanted if they also believe that person is using a fraudulent passport. In two experiments, undergraduate students assumed the role of a border control officer and completed multiple "shifts" of a face matching task designed to simulate a passport verification check. Before each shift participants viewed posters of wanted people and were instructed to report any sightings if a wanted person appeared in any of the images during the passport check. Participants were more likely to say an individual was wanted if they also believed the person did not match their passport image. In addition, the accuracy of wanted person sightings was reduced for trials with nonmatching passports compared to trials with matching passports. This suggests wanted people with matching passports were easier to spot because participants had an additional image to compare with their memory of the person in the wanted poster.

Objective: The risk of mistaken identification for innocent suspects in lineups can be estimated by correcting the overall error rate by the number of people in the lineup. We compared this nominal size correction to a new effective size correction, which adjusts the error rate for the number of plausible lineup members., Hypotheses: We hypothesized that (a) increasing lineup bias would increase misidentifications of a designated innocent suspect; (b) with the effective size correction, increasing lineup bias would also increase the estimate of innocent-suspect misidentifications; and (c) with the nominal size correction, lineup bias would have no effect on the estimate of innocent-suspect misidentifications., Method: In a reanalysis of previous literature, we obtained 10 data sets from Open Science Framework. In three new experiments ( Ns = 686, 405, and 1,531, respectively), participants observed a staged crime and completed a fair or biased lineup., Results: In the reanalysis of previous literature, less than four of six lineup members were identified frequently enough to be classified as plausible, M = 3.78, 95% confidence interval [CI: 2.20, 5.36]. In the new experiments, increasing lineup bias increased mistaken identifications of a designated innocent suspect, odds ratio ( OR ) = 5.50, 95% CI [2.77, 10.95] and also increased the effective size-corrected estimate of innocent-suspect misidentifications, OR = 3.04, 95% CI [2.13, 4.33]. With the nominal size correction, lineup bias had no effect on the estimate of innocent-suspect misidentifications, OR = 0.84, 95% CI [0.60, 1.18]., Conclusions: Most lineups include a combination of plausible and implausible lineup members. Contrary to the nominal size correction, which ignores implausible lineup members, the effective size correction is sensitive to implausible lineup members and accounts for lineup bias when estimating the risk of innocent suspect misidentifications. (PsycInfo Database Record (c) 2023 APA, all rights reserved).

Introduction: Sprat ( Sprattus sprattus ) is an underutilized fish species that may act as an economic and sustainable alternative source of protein due to its good amino acid (AA) profile along with its potential to act as a source of multiple bioactive peptide sequences., Method and Results: This study characterized the physicochemical, technofunctional, and in vitro antioxidant properties along with the AA profile and score of a sprat protein enzymatic hydrolysate (SPH). Furthermore, the impact of the SPH on the growth, proliferation, and muscle protein synthesis (MPS) in skeletal muscle (C2C12) myotubes was examined. The SPH displayed good solubility and emulsion stabilization properties containing all essential and non-essential AAs. Limited additional hydrolysis was observed following in vitro- simulated gastrointestinal digestion (SGID) of the SPH. The SGID-treated SPH (SPH-SGID) displayed in vitro oxygen radical antioxidant capacity (ORAC) activity (549.42 μmol TE/g sample) and the ability to reduce (68%) reactive oxygen species (ROS) production in C2C12 myotubes. Muscle growth and myotube thickness were analyzed using an xCELLigence™ platform in C2C12 myotubes treated with 1 mg protein equivalent.mL -1 of SPH-SGID for 4 h. Anabolic signaling (phosphorylation of mTOR, rpS6, and 4E-BP1) and MPS (measured by puromycin incorporation) were assessed using immunoblotting. SPH-SGID significantly increased myotube thickness ( p < 0.0001) compared to the negative control (cells grown in AA and serum-free medium). MPS was also significantly higher after incubation with SPH-SGID compared with the negative control ( p < 0.05)., Conclusions: These preliminary in situ results indicate that SPH may have the ability to promote muscle enhancement. In vivo human studies are required to verify these findings., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (Copyright © 2023 Shekoohi, Naik, Amigo-Benavent, Harnedy-Rothwell, Carson and FitzGerald.)

Blue whiting (BW) represents an underutilised fish species containing a high-quality protein and amino acid (AA) profile with numerous potentially bioactive peptide sequences, making BW an economic and sustainable alternative source of protein. This study investigated the impact of three different BW protein hydrolysates (BWPH-X, Y and Z) on growth, proliferation and muscle protein synthesis (MPS) in skeletal muscle (C2C12) myotubes. BWPHs were hydrolysed using different enzymatic and heat exposures and underwent simulated gastrointestinal digestion (SGID), each resulting in a high degree of hydrolysis (33.41-37.29%) and high quantities of low molecular mass peptides (86.17-97.12% <1 kDa). C2C12 myotubes were treated with 1 mg protein equivalent/mL of SGID-BWPHs for 4 h. Muscle growth and myotube thickness were analysed using an xCelligence™ platform. Anabolic signalling (phosphorylation of mTOR, rpS6 and 4E-BP1) and MPS measured by puromycin incorporation were assessed using immunoblotting. BWPH-X significantly increased muscle growth ( p < 0.01) and myotube thickness ( p < 0.0001) compared to the negative control (amino acid and serum free media). Muscle protein synthesis (MPS), as measured by puromycin incorporation, was significantly higher after incubation with BWPH-X compared with the negative control, but did not significantly change in response to BWPH-Y and Z treatments. Taken together, these preliminary findings demonstrate the anabolic potential of some but not all BWPHs on muscle enhancement, thus providing justification for human dietary intervention studies to confirm and translate the results of such investigations to dietary recommendations and practices.

The proteins from two conventionally (CC1 and CC2) and one organically cultivated (OC) hempseed samples were extracted (by alkaline solubilization followed by isoelectric precipitation) and compared in terms of their physicochemical, digestibility and in vitro bioactivity properties. The OC hempseed had higher total protein and lower nonprotein nitrogen content. Protein extracts showed bimodal particle size distributions, with OC showing the smallest and CC1 the largest mean particle diameter (d(0.5)), i.e., 89.0 and 120.0 µm, respectively. Chromatographic analysis showed similar protein profiles for all three protein extracts. The protein extracts were subjected to in vitro simulated gastrointestinal digestion (SGID). Degree of hydrolysis (DH) measurement showed that the highest extent of digestion upon SGID was associated with CC1 (11.0 ± 1.5%), which also had the lowest in vitro antioxidant activity. Only the OC and OC digested samples had lipase inhibitory activity. The results indicate that the cultivation method impacted the composition, physicochemical, digestibility, and biofunctional properties of hempseed proteins.

This study investigated the characterization of proteins from the Irish limpet ( Patella vulgata ) and assessed the in vitro biological activities of hydrolysates obtained following gastrointestinal digestion (INFOGEST) of a limpet protein concentrate (LPC). The physicochemical properties and the digestibility of the LPC were investigated, along with the angiotensin-converting enzyme (ACE) inhibition and antioxidant activities of the LPC-digested samples. All the digested samples examined outperformed the LPC in terms of activity. Peptides were identified using LC-MS/MS after digestion. A total of 38 and 19 peptides were identified in LPC-G and LPC-GI, respectively, using a database search and a de novo approach. Most of the identified peptides had hydrophobic amino acids, which may contribute to their antioxidant and ACE inhibitory activities. The findings of this study showed that LPC has high nutritional quality with good digestibility and could serve as a potential source of antioxidative and ACE inhibitory peptides following gastrointestinal digestion.

Dipeptidyl-peptidase IV (DPP-IV) plays an essential role in glucose metabolism by inactivating incretins. In this context, food-protein-derived DPP-IV inhibitors are promising glycemic regulators which may act by preventing the onset of type 2 diabetes in personalized nutrition. In this study, the DPP-IV-inhibitory potential of seven proteins from diverse origins was compared for the first time in vitro and in vivo in rat plasma after the intestinal barrier (IB) passage of the indigested proteins. The DPP-IV-inhibitory potentials of bovine hemoglobin, caseins, chicken ovalbumin, fish gelatin, and pea proteins were determined in rat plasma thirty minutes after oral administration. In parallel, these proteins, together with bovine whey and gluten proteins, were digested using the harmonized INFOGEST protocol adapted for proteins. The DPP-IV half-maximal inhibitory concentration (IC 50 ) was determined in situ using Caco-2 cells. The DPP-IV-inhibitory activity was also measured after IB passage using a Caco2/HT29-MTX mixed-cell model. The peptide profiles were analyzed using reversed-phase high-performance liquid chromatography tandem mass spectrometry (RP-HPLC-MS/MS) with MS data bioinformatics management, and the IC 50 of the identified peptides was predicted in silico. The in vitro and in vivo DPP-IV-inhibitory activity of the proteins differed according to their origin. Vegetable proteins and hemoglobin yielded the highest DPP-IV-inhibitory activity in vivo. However, no correlation was found between the in vivo and in vitro results. This may be partially explained by the differences between the peptidome analysis and the in silico predictions, as well as the study complexity.

During the generation of functional food ingredients by enzymatic hydrolysis, parameters such as choice of enzyme, reaction pH and the drying process employed may contribute to the physicochemical and bio-functional properties of the resultant protein hydrolysate ingredients. This study characterised the properties of spray- (SD) and freeze-dried (FD) whey protein hydrolysates (WPHs) generated using Alcalase ® and Prolyve ® under pH-stat and free-fall pH conditions. The enzyme preparation used affected the physicochemical and antioxidative properties but had no impact on powder composition, morphology or colour. SD resulted in spherical particles with higher moisture content (~6%) compared to the FD powders (~1%), which had a glass shard-like structure. The SD-WPHs exhibited higher antioxidative properties compared to the FD-WPHs, which may be linked to a higher proportion of peptides <1 kDa in the SD-WPHs. Furthermore, the SD- and FD-WPHs had similar peptide profiles, and no evidence of Maillard reaction product formation during the SD processing was evident. The most potent in vitro antioxidative WPH was generated using Alcalase ® under free-fall pH conditions, followed by SD, which had oxygen radical absorbance capacity and Trolox equivalent (TE) antioxidant capacity values of 1132 and 686 µmol TE/g, respectively. These results demonstrate that both the hydrolysis and the drying process impact the biofunctional (antioxidant) activity of WPHs.

This study determined the physicochemical properties (apparent viscosity (η app ), turbidity (A 550nm ), particle size and molecular mass distribution) of hydrolysates generated from whey protein concentrate (WPC), milk protein concentrate (MPC) and sodium caseinate (NaCN), following incubation with Debitrase HYW20™ and Prolyve™ at 50 °C, pH 7.0 for 1 and 4 h, before and after heat inactivation (80 °C for 10 min). The degree of hydrolysis (DH) increased with incubation time, giving values of 6.56%, 8.17% and 9.48%, following 1 h hydrolysis of WPC, MPC and NaCN with Debitrase HYW20™, and 12.04%, 15.74% and 17.78%, respectively, following 4 h incubation. These DHs were significantly higher compared to those obtained following 4 h incubation with Prolyve™. Hydrolysis with Debitrase HYW20™ gave >40% of peptides with molecular masses < 1 kDa for all substrates, which was higher than the value obtained following hydrolysis with Prolyve™. The effect of hydrolysis on the physicochemical properties was substrate dependent, since η app decreased in WPC and NaCN hydrolysates, particle size decreased for all the substrates, with aggregate formation for MPC, and turbidity decreased in WPC and MPC hydrolysates, while it increased in NaCN hydrolysates. The physical properties of the hydrolysates were influenced by the enzyme thermal inactivation step in a DH-dependent manner, with no significant effect on turbidity and viscosity for hydrolysates at higher DHs.

Inducing the feeling of fullness via the regulation of satiety hormones presents an effective method for reducing excess energy intake and, in turn, preventing the development of obesity. In this study, the ability of blue whiting soluble protein hydrolysates (BWSPHs) and simulated gastrointestinal digested (SGID) BWSPHs, to modulate the secretion and/or production of satiety hormones, such as glucagon-like peptide-1 (GLP-1), cholecystokinin (CCK) and peptide YY (PYY), was assessed in murine enteroendocrine STC-1 cells. All BWSPHs (BW-SPH-A to BW-SPH-F) (1.0% w / v dw) increased active GLP-1 secretion and proglucagon production in STC-1 cells compared to the basal control (Krebs-Ringer buffer) ( p < 0.05). The signaling pathway activated for GLP-1 secretion was also assessed. A significant increase in intracellular calcium levels was observed after incubation with all BWSPHs ( p < 0.05) compared with the control, although none of the BWSPHs altered intracellular cyclic adenosine monophosphate (cAMP) concentrations. The secretagogue effect of the leading hydrolysate was diminished after SGID. Neither pre- nor post-SGID hydrolysates affected epithelial barrier integrity or stimulated interleukin (IL)-6 secretion in differentiated Caco-2/HT-29MTX co-cultured cells. These results suggest a role for BWSPH-derived peptides in satiety activity; however, these peptides may need to be protected by some means to avoid loss of activity during gastrointestinal transit.

Cow (CwC) and camel casein (CaC) hydrolysates were generated using Alcalase™ (CwCA and CaCA) and Pronase-E (CwCP and CaCP) each for 3 and 6 h, and investigated for their potential to inhibit key lipid digesting enzymes i.e., pancreatic lipase (PL) and cholesteryl esterase (CE). Results revealed stronger PL and CE inhibition by CaC hydrolysates compared to CwC. Potent hydrolysates (CwCP-3 h and CaCA-6 h) upon simulated gastrointestinal digestion (SGID) showed significant improvement in inhibition of both PL and CE. However, both the SGID hydrolysates showed similar extent of PL and CE inhibition and were further sequenced for peptide identification. Peptides MMML, FDML, HLPGRG from CwC and AAGF, MSNYF, FLWPEYGAL from CaC hydrolysates were predicted to be most active PL inhibitory peptides. Peptide LP found in both CwC and CaC hydrolysates was predicted as active CE inhibitor. Thus, CwC and CaC could be potential source of peptides with promising CE and PL inhibitory properties., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

Milk protein concentrates (MPCs), which are produced from skim milk following a series of manufacturing steps including pasteurization, membrane filtration, evaporation and spray drying, represent a relatively new category of dairy ingredients. MPC powders mainly comprise caseins and whey proteins in the same ratio of occurrence as in milk. While bovine MPCs have applications as an ingredient in several protein enriched food products, technofunctional concerns, e.g., reduced solubility and emulsification properties, especially after long-term storage, limit their widespread and consistent utilization in many food products. Changes in the surface and internal structure of MPC powder particles during manufacture and storage occur via casein-casein and casein-whey protein interactions and also via the formation of casein crosslinks in the presence of calcium ions which are associated with diminishment of MPCs functional properties. The aggregation of micellar caseins as a result of these interactions has been considered as the main cause of insolubility in MPCs. In addition, the occurrence of lactose-protein interactions as a result of the promotion of the Maillard reaction mainly during storage of MPC may lead to greater insolubility. This review focuses on the solubility of MPC with an emphasis on understanding the factors involved in its insolubility along with approaches which may be employed to overcome MPC insolubility. Several strategies have been developed based on manipulation of the manufacturing process, along with composition, physical, chemical and enzymatic modifications to overcome MPC insolubility. Despite many advances, dairy ingredient manufacturers are still investigating technical solutions to resolve the insolubility issues associated with the large-scale manufacture of MPC.

Dietary proteins are involved in the regulation of glucose homeostasis by different mechanisms. Food protein digestion products are reported to inhibit dipeptidyl peptidase IV (DPP-IV), induce incretin secretion or directly exert an insulinotropic effect in pancreatic β-cells. This study illustrates the DPP-IV inhibitory activity of gastric and intestinal digests of casein, whey and egg white proteins determined in vitro , using Gly-Pro-AMC, and in situ using non-differentiated Caco-2 cells. Comparable trends in the DPP-IV inhibitory profiles were obtained by these two methods although the extent of inhibition in situ was consistently lower than the inhibition observed in vitro . Casein intestinal digests and whey protein gastric and intestinal digests showed potent DPP-IV inhibitory activities in Caco-2 cells with IC 50 values ranging from 0.8 to 1.2 mg mL -1 . The absorbed fraction of the intestinal digests from whey and egg white protein induced insulin secretion in BRIN-BD11 cells when determined using a two-tiered cellular model (Caco-2 and BRIN-BD11). However, the gastric digests from the same substrates showed no insulin secretion. This may be related to limited trans-epithelial transport through the Caco-2 monolayer of the gastric digestion products. However, both, gastric and intestinal digests were able to induce insulin secretion in BRIN-BD11 cells when the monolayer was composed of a co-culture of STC-1 and Caco-2 cells. This result may be attributed to the activation of STC-1 cells and subsequent incretin secretion, induced by the gastric digest, as shown by an enhanced intracellular calcium uptake.

Purpose: This study investigated metabolic benefits of protein hydrolysates from the macroalgae Palmaria palmata, previously shown to inhibit dipeptidylpeptidase-4 (DPP-4) activity in vitro., Methods: Previously, Alcalase/Flavourzyme-produced P. palmata protein hydrolysate (PPPH) improved glycaemia and insulin production in streptozotocin-induced diabetic mice. Here the PPPH, was compared to alternative Alcalase, bromelain and Promod-derived hydrolysates and an unhydrolysed control. All PPPH's underwent simulated gastrointestinal digestion (SGID) to establish oral bioavailability. PPPH's and their SGID counterparts were tested in pancreatic, clonal BRIN-BD11 cells to assess their insulinotropic effect and associated intracellular mechanisms. PPPH actions on the incretin effect were assessed via measurement of DPP-4 activity, coupled with GLP-1 and GIP release from GLUTag and STC-1 cells, respectively. Acute in vivo effects of Alcalase/Flavourzyme PPPH administration on glucose tolerance and satiety were assessed in overnight-fasted mice., Results: PPPH's (0.02-2.5 mg/ml) elicited varying insulinotropic effects (p < 0.05-0.001). SGID of the unhydrolysed protein control, bromelain and Promod PPPH's retained, or improved, bioactivity regarding insulin secretion, DPP-4 inhibition and GIP release. Insulinotropic effects were retained for all SGID-hydrolysates at higher PPPH concentrations. DPP-4 inhibitory effects were confirmed for all PPPH's and SGID counterparts (p < 0.05-0.001). PPPH's were shown to directly influence the incretin effect via upregulated GLP-1 and GIP (p < 0.01-0.001) secretion in vitro, largely retained after SGID. Alcalase/Flavourzyme PPPH produced the greatest elevation in cAMP (p < 0.001, 1.7-fold), which was fully retained post-SGID. This hydrolysate elicited elevations in intracellular calcium (p < 0.01) and membrane potential (p < 0.001). In acute in vivo settings, Alcalase/Flavourzyme PPPH improved glucose tolerance (p < 0.01-0.001) and satiety (p < 0.05-0.001)., Conclusion: Bioavailable PPPH peptides may be useful for the management of T2DM and obesity., (© 2021. The Author(s).)

The use of plant-derived proteins in the generation of food products is gaining popularity as an alternative to proteins of animal origin. This study described the emulsifying and bioactive properties of fava bean protein hydrolysates (FBH) generated at low and high degree of hydrolysis (DH), i.e., FBH 8 (low DH: 8.4 ± 0.3) and FBH 210 (high DH: 15.6 ± 0.7) when adjusted to three different pHs (3.0, 5.0 and 8.0). Overall, FBH 8 , had more favourable emulsifying properties compared to the FBH 210. The emulsion generated with FBH 8 at pH 8.0 also had the highest antioxidant activity when measured by the oxygen radical absorbance capacity (ORAC) and ferric reducing antioxidant power (FRAP) assays with values of 1108.6 ± 3.8 and 1159.9 ± 20.5 μmol Trolox Eq·g -1 emulsion, respectively. The antioxidant activity of the emulsions, in most cases, remained unchanged following in vitro simulated gastrointestinal digestion. Both the FBH 8 and FBH 210 emulsions following in vitro simulated gastrointestinal digestion were able to inhibit the activities of dipeptidyl peptidase-IV (DPP-IV) and angiotensin converting enzyme (ACE) with ∼45% and 65% inhibition, respectively. These results indicated that hydrolysates from fava bean may find use for the generation of bioactive emulsions., (Copyright © 2021 Elsevier Ltd. All rights reserved.)