-
European Archives of... Aug 2023To study the diagnostic value of salivary pepsin measurement (Peptest) for detecting gastroesophageal reflux disease (GERD) in laryngopharyngeal reflux (LPR) patients.
OBJECTIVE
To study the diagnostic value of salivary pepsin measurement (Peptest) for detecting gastroesophageal reflux disease (GERD) in laryngopharyngeal reflux (LPR) patients.
METHODS
Patients with reflux symptoms were consecutively recruited from January 2020 to November 2022. Patients benefited from hypopharyngeal-esophageal impedance-pH monitoring (HEMII-pH), fasting and bedtime saliva collections to measure pepsin. Sensitivity, specificity, positive (PPV) and negative (NPV) predictive values were evaluated for GERD and LPR patients considering the highest values of pepsin tests at ≥ 16, ≥ 75, and ≥ 216 ng/mL cutoffs. The relationship between HEMII-pH, endoscopic and clinical findings, and pepsin measurements was studied.
RESULTS
Saliva was collected in 109 LPR patients and 30 individuals with both LPR and GERD. The total number of pharyngeal reflux events was significantly higher in GERD-LPR patients compared with LPR patients (p = 0.008). The mean fasting and bedtime pepsin saliva concentrations were similar between groups. The sensitivity of Peptest in LPR patients was 30.5%, 70.2%, and 84.0% at cutoffs ≥ 16, ≥ 75 and ≥ 216 ng/mL. In GERD-LPR group, Peptest was 80.0%, 70.0%, and 30.0% sensitive. At cutoff 16 ng/mL, Peptest reported PPV of 20.7% and 94.8% in LPR-GERD and LPR groups, respectively. NPV were 73.9% and 8.7% in GERD-LPR and LPR groups, respectively. The consistency analysis between Peptest and HEMII-pH was not significant. Peptest was significantly associated with the number of acid pharyngeal reflux events (r = 0.182; p = 0.032).
CONCLUSION
Pepsin saliva measurements appear to be not a reliable diagnostic tool for the detection of GERD in LPR patients. Future studies are needed to determine the place of Peptest in laryngopharyngeal reflux and gastroesophageal reflux diseases.
Topics: Humans; Laryngopharyngeal Reflux; Pepsin A; Cohort Studies; Saliva; Esophageal pH Monitoring
PubMed: 37140740
DOI: 10.1007/s00405-023-08000-1 -
Food Chemistry Dec 2023The stability behaviors of oxidized SPI emulsions under in vitro gastric conditions and the effects of pepsin diffusion on the proteolysis of emulsions were investigated...
The stability behaviors of oxidized SPI emulsions under in vitro gastric conditions and the effects of pepsin diffusion on the proteolysis of emulsions were investigated using a static gastric model and the fluorescence recovery after photobleaching method. Results showed that protein oxidation increased the particle size of droplets and decreased the viscoelasticity of the interfacial layer. Compared to the control group (82.81 m/s), the pepsin diffusivity decreased to 68.52 m/s (7LA + LOX group) due to the space hindrance of oil droplets. After gastric digestion, protein hydrolysates were re-absorbed on the oil-water interface and formed a thick layer, thereby decreasing the size of oil droplets and reducing the contents of free amino acids in gastric digesta. The protein oxidation may affect the adsorption of interfacial proteins and alter the distribution of droplets, decreasing pepsin diffusion and ultimately impairing the emulsion gastric digestion. And this should be considered in the design of emulsion as the controllable delivery system.
Topics: Pepsin A; Emulsions; Stomach; Proteins; Particle Size; Digestion
PubMed: 37429241
DOI: 10.1016/j.foodchem.2023.136791 -
Food Research International (Ottawa,... Aug 2023Hydrophilic polysaccharides have been widely applied as fat replacers in meat products, but their effects on the digestibility of meat proteins has seldom been studied....
Hydrophilic polysaccharides have been widely applied as fat replacers in meat products, but their effects on the digestibility of meat proteins has seldom been studied. Replacement of backfat in emulsion-type sausage with konjac gum (KG), sodium alginate (SA) and xanthan gum (XG) were found to reduce the released amino group (-NH) during simulated gastric digestion and initial intestinal digestion. The suppressed gastric digestibility of protein was verified by the denser structures of protein gastric digests and reduced generation of peptides in gastric digestion when a polysaccharide was added. After the whole gastrointestinal digestion, high level of SA and XG resulted in larger digests and a more obvious SDS-PAGE band between 5 and 15 kDa, and KG and SA significantly reduced the total release of -NH. Additional of KG, SA and XG were found to the increase the viscosity of the gastric digests mixture, which could account for the reduced hydrolysis efficiency of pepsin during the gastric digestion, as evidenced in the pepsin activity study (decreased by 12.2-39.1%). This work highlights the influence of polysaccharide fat replacer on the digestibility of meat protein by changing the matrix characteristics.
Topics: Emulsions; Meat Products; Pepsin A; Polysaccharides; Alginates; Amorphophallus; Meat Proteins
PubMed: 37316076
DOI: 10.1016/j.foodres.2023.113008 -
Molecules (Basel, Switzerland) Mar 2024Pepsin, trypsin and proteinase K were used in the present study to hydrolyse the proteins from whole eggs, yolks or whites, and the resulting hydrolysates were...
Pepsin, trypsin and proteinase K were used in the present study to hydrolyse the proteins from whole eggs, yolks or whites, and the resulting hydrolysates were characterised in terms of antioxidant and IgE-binding properties, using a combination of in vitro and in silico methods. Based on the degree of hydrolysis (DH) results, the egg yolk proteins are better substrates for all the tested enzymes (DH of 6.2-20.1%) compared to those from egg whites (DH of 2.0-4.4%). The SDS-PAGE analysis indicated that pepsin and proteinase K were more efficient compared to trypsin in breaking the intramolecular peptide bonds of the high molecular weight egg proteins. For all the tested substrates, enzyme-assisted hydrolysis resulted in a significant increase in antioxidant activity, suggesting that many bioactive peptides are encrypted in inactive forms in the parent proteins. The hydrolysates obtained with proteinase K exhibited the highest DPPH radical scavenging activity (124-311 µM Trolox/g protein) and the lowest residual IgE-binding capacity. The bioinformatics tools revealed that proteinase K is able to break the integrity of the main linear IgE-binding epitopes from ovalbumin and ovomucoid. It can be concluded that proteinase K is a promising tool for modulating the intrinsic properties of egg proteins.
Topics: Antioxidants; Pepsin A; Trypsin; Endopeptidase K; Peptides; Egg Proteins; Hydrolysis; Immunoglobulin E; Protein Hydrolysates
PubMed: 38542963
DOI: 10.3390/molecules29061327 -
The British Journal of Nutrition Sep 2023For the omnivorous crayfish, plant raw materials can be good alternatives to dietary fish meal (FM). A 56-d feeding trial was conducted in (11·70 (se 0·13) g). Diet...
Effects of dietary plant protein sources intake on growth, digestive enzyme activity, edible tissue nutritional status and intestinal health of the omnivorous Redclaw crayfish, .
For the omnivorous crayfish, plant raw materials can be good alternatives to dietary fish meal (FM). A 56-d feeding trial was conducted in (11·70 (se 0·13) g). Diet with 100 % FM as the protein source was the control. Seven experimental diets were formulated by replacing 75 or 100 % of FM with soyabean meal (SM75, SM100) or cottonseed meal (CM75 and CM100), and a mixture of SM and CM (protein content is 1:1) replacing 50, 75 or 100 % of FM (SC50, SC75 and SC100). Crayfish fed the CM100 and SC100 showed significantly lower weight gain (WG), specific growth rate, trypsin and pepsin activities compared with the control diet. Crayfish in CM100 group showed significantly higher GPx, alanine aminotransferase, aspartate aminotransferase activities and malondialdehyde content than the control. SM100 and CM100 diets can cause slight separation of the peritrophic membrane from the intestinal folds. The pepsin activity of crayfish in SC50 was significantly higher than those in other experimental diets. The highest WG and muscle arginine content were also found in crayfish fed SC50. The relative abundance of , and was significantly higher, but was significantly lower in SM100, CM100 and SC100 than in control. Microbiota functional prediction indicated that the relative abundance of 'cell motility' pathway in crayfish fed CM100 was significantly decreased compared with the control. In conclusion, only half of the FM can be effectively substituted with a mixture of SM and CM (protein content is 1:1) for .
Topics: Animals; Astacoidea; Nutritional Status; Plant Proteins, Dietary; Pepsin A; Intestines; Diet; Animal Feed
PubMed: 36597816
DOI: 10.1017/S0007114522004044 -
Marine Drugs Dec 2023Fish head byproducts derived from surimi processing contribute about 15% of the total body weight, which are beneficial to health because they contain essential...
Pepsin Hydrolysate from Surimi Industry-Related Olive Flounder Head Byproducts Attenuates LPS-Induced Inflammation and Oxidative Stress in RAW 264.7 Macrophages and In Vivo Zebrafish Model.
Fish head byproducts derived from surimi processing contribute about 15% of the total body weight, which are beneficial to health because they contain essential nutrients. In this study, olive flounder (OF) was the target species in order to maximize the byproduct utilization. In RAW 264.7 macrophages, the seven hydrolysates from OF head byproducts were examined for their inhibitory potential against inflammation and the oxidative stress induced by lipopolysaccharides (LPS). The pepsin hydrolysate (OFH-PH) demonstrated strong anti-inflammatory activity via the down-regulation of NO production, with an IC50 value of 299.82 ± 4.18 µg/mL. We evaluated the inhibitory potential of pro-inflammatory cytokines and PGE2 to confirm these findings. Additionally, iNOS and COX-2 protein expressions were confirmed using western blotting. Furthermore, the results from the in vivo zebrafish model demonstrated that OFH-PH decreased the LPS-elevated heart rate, NO production, cell death, and intracellular ROS level, while increasing the survival percentage. Hence, the obtained results of this study serve as a platform for future research and provide insight into the mediation of inflammatory disorders. These results suggest that OFH-PH has the potential to be utilized as a nutraceutical and functional food ingredient.
Topics: Animals; Zebrafish; Flounder; Lipopolysaccharides; Pepsin A; Inflammation; Perciformes; Oxidative Stress; Macrophages
PubMed: 38248649
DOI: 10.3390/md22010024 -
Protein Expression and Purification Apr 2024Human pepsinogens (mainly pepsinogen I and pepsinogen II) are the major inactive precursor forms of the digestive enzyme pepsin which play a crucial role in protein...
Human pepsinogens (mainly pepsinogen I and pepsinogen II) are the major inactive precursor forms of the digestive enzyme pepsin which play a crucial role in protein digestion. The levels and ratios of human pepsinogens have demonstrated potential as diagnostic biomarkers for gastrointestinal diseases, particularly gastric cancer. Nanobodies are promising tools for the treatment and diagnosis of diseases, owing to their unique recognition properties. In this study, recombinant human pepsinogens proteins were expressed and purified as immunized antigens. We constructed a VHH phage library and identified several nanobodies via phage display bio-panning. We determined the binding potency and cross-reactivity of these nanobodies. Our study provides technical support for developing immunodiagnostic reagents targeting human pepsinogens.
Topics: Humans; Pepsinogens; Single-Domain Antibodies; Gastric Mucosa; Pepsin A
PubMed: 38184161
DOI: 10.1016/j.pep.2024.106431 -
Food Research International (Ottawa,... Jun 2024In this article, the synthesis of antioxidant peptides in the enzymatic hydrolysis of caprine casein was analyzed at three different time points (60 min, 90 min, and...
In this article, the synthesis of antioxidant peptides in the enzymatic hydrolysis of caprine casein was analyzed at three different time points (60 min, 90 min, and 120 min) using immobilized pepsin on activated and modified carbon (AC, ACF, ACG 50, ACG 100). The immobilization assays revealed a reduction in the biocatalysts' activity compared to the free enzyme. Among the modified ones, ACG 50 exhibited greater activity and better efficiency for reuse cycles, with superior values after 60 min and 90 min. Peptide synthesis was observed under all studied conditions. Analyses (DPPH, β-carotene/linoleic acid, FRAP) confirmed the antioxidant potential of the peptides generated by the immobilized enzyme. However, the immobilized enzyme in ACG 50 and ACG 100, combined with longer hydrolysis times, allowed the formation of peptides with an antioxidant capacity greater than or equivalent to those generated by the free enzyme, despite reduced enzymatic activity.
Topics: Antioxidants; Enzymes, Immobilized; Goats; Caseins; Animals; Pepsin A; Glutaral; Peptides; Iridoids; Hydrolysis; Charcoal
PubMed: 38729685
DOI: 10.1016/j.foodres.2024.114161 -
Food Research International (Ottawa,... Jul 2024Oral delivery of larger bioactive peptides (>20 amino acids) to the small intestine remains a challenge due to their sensitivity to proteolytic degradation and chemical...
Oral delivery of larger bioactive peptides (>20 amino acids) to the small intestine remains a challenge due to their sensitivity to proteolytic degradation and chemical denaturation during gastrointestinal transit. In this study, we investigated the capacity of crosslinked alginate microcapsules (CLAMs) formed by spray drying to protect Plantaricin EF (PlnEF) (C-EF) in gastric conditions and to dissolve and release PlnEF in the small intestine. PlnEF is an unmodified, two-peptide (PlnE: 33 amino acids; PlnF: 34 amino acids) bacteriocin produced by Lactiplantibacillus plantarum with antimicrobial and gut barrier protective properties. After 2 h incubation in simulated gastric fluid (SGF) (pH 1.5), 43.39 % ± 8.27 % intact PlnEF was liberated from the CLAMs encapsulates, as determined by an antimicrobial activity assay. Transfer of the undissolved fraction to simulated intestinal fluid (SIF) (pH 7) for another 2 h incubation resulted in an additional release of 16.13 % ± 4.33 %. No active PlnEF was found during SGF or sequential SIF incubations when pepsin (2,000 U/ml) was added to the SGF. To test PlnEF release in C-EF contained in a food matrix, C-EF was mixed in peanut butter (PB) (0.15 g C-EF in 1.5 g PB). A total of 12.52 % ± 9.09 % active PlnEF was detected after incubation of PB + C-EF in SGF without pepsin, whereas no activity was found when pepsin was included. Transfer of the remaining PB + C-EF fractions to SIF yielded the recovery of 46.67 % ± 13.09 % and 39.42 % ± 11.53 % active PlnEF in the SIF following exposure to SGF and to SGF with pepsin, respectively. Upon accounting for the undissolved fraction after SIF incubation, PlnEF was fully protected in the CLAMs-PB mixture and there was not a significant reduction in active PlnEF when pepsin was present. These results show that CLAMs alone do not guard PlnEF bacteriocin peptides from gastric conditions, however, mixing them in PB protected against proteolysis and improved intestinal release.
Topics: Alginates; Bacteriocins; Capsules; Peptides; Intestine, Small; Lactobacillus plantarum; Hydrogen-Ion Concentration; Cross-Linking Reagents; Pepsin A
PubMed: 38823837
DOI: 10.1016/j.foodres.2024.114473 -
European Archives of... Feb 2024To study the diagnostic value of salivary pepsin tests for detecting laryngopharyngeal reflux (LPR) in patients with primary burning mouth syndrome (BMS).
OBJECTIVES
To study the diagnostic value of salivary pepsin tests for detecting laryngopharyngeal reflux (LPR) in patients with primary burning mouth syndrome (BMS).
METHODS
Patients with BMS and asymptomatic individuals were consecutively recruited from September 2018 to June 2023. Patients underwent hypopharyngeal-esophageal impedance pH-monitoring (HEMII-pH) and saliva collections to measure pepsin. Stomatology evaluation was carried out to exclude other causes of BMS. Oral, pharyngeal and laryngeal signs and symptoms were evaluated with Reflux Sign Assessment (RSA) and Reflux Symptom Score (RSS). Sensitivity, specificity, positive (PPV) and negative (NPV) predictive values of pepsin test were calculated considering the highest values of pepsin tests at ≥ 16, ≥ 36, and ≥ 100 ng/mL cutoffs. Receiver operating characteristic curve (ROC) was evaluated.
RESULTS
Forty-nine patients with both BMS and LPR at the HEMII-pH and 21 asymptomatic individuals were recruited. Pepsin test was 83.7%, 79.6%, and 71.4% sensitive at cutoffs ≥ 16, ≥ 36, and ≥ 100 ng/mL, respectively. The ROC analysis reported that a threshold of ≥ 21.5 ng/mL was associated with sensitivity, specificity, PPV and NPV of 81.6%, 81.0%, 90.1% and 65.4%, respectively. The severity score of burning mouth symptom was significantly associated with the saliva pepsin concentration (r = 0.263; p = 0.029) and the oral RSA (r = 0.474; p = 0.007).
CONCLUSION
Pepsin test is a valuable diagnostic approach for detecting LPR in patients with BMS. Patients with high level of saliva pepsin reported more severe burning mouth symptoms. Future studies are needed to confirm the role of LPR in the primary BMS.
Topics: Humans; Saliva; Pepsin A; Burning Mouth Syndrome; Prospective Studies; Esophageal pH Monitoring; Laryngopharyngeal Reflux; Electric Impedance
PubMed: 37906367
DOI: 10.1007/s00405-023-08317-x