Noise is considered as one of the most severe sources of environmental and workplace constraints. Many noise effects are well known on immune function, hormonal levels, cardiovascular and respiratory systems. In this study, our aim is to evaluate the effects of traffic noise exposure on basal and stimulated gastric PEPSIN secretion.48 male rats were exposed to traffic noise (86 dB) for a short term of (8h/ day for 1 day) and a long term of (8h/ day for 7, 14, 21 and 28 days) as well as a control group. The gastric contents were collected by the wash-out technique. PEPSIN secretion was measured by employing the Anson method. Histological studies were carried out on the epithelial layer. The corticosteroid hormone was measured in the serum for the stress augmentation. The present finding indicated no changes in PEPSIN secretion content in the short term, but in the 14 and 21 days traffic noise exposure, basal gastric PEPSIN secretion increased markedly compared to the control group. Histological results showed that the number of oxyntic glands and cell nuclei decreased in comparison with the control group while the thickness of the epithelial layer increases. In addition, the corticosterone levels increase in all groups in comparison with the control. It seems that the increase of gastric PEPSIN secretion is due to the description and translation processes in the peptic cells and needs enough time for completion.

Collagen, which is widely distributed in pluricellular animals, is one of the most fundamental constituents of the extracellular matrix, and plays mechanically or physiologically important roles in their bodies. In this study, the biochemical and physical characteristics of PEPSIN-solubilized collagen from the mantle of Yesso scallop (YMPC), a by-product of processing, was determined. Electrophoretic patterns showed that scallop mantle collagen contained a1 and a2 chains, which was similar to the patterns of bovine tendon type V collagen. The YMPC showed different profiles in molecular, amino acids, peptide maps from those of bovine tendon collagen and lower denaturation temperature. Electron microscopic view of YMPC showed a sponge-like structure in part. These results indicated that YMPC may become a sustainable source of useful collagens for various purposes including value-added biomaterials. It may also be useful in a variety of applications as an alternative of vertebrate collagen, which has been widely used.

PEPSIN (E.C.3.4.23.1) is a juice gastric aspartic proteinase. It belongs to hydrolyses family. Its monomeris structure is consisting of two lobes that they are similar in size and folding. It consists of a single polypeptide chain of molecular weight 34644 Dalton and 327 amino acids. Structural analysis shows that PEPSIN contains 1.2% basic residues, 13.1% acidic residues, 46.5% polar residues and 39.2% hydrophobic residues. Structural stability of PEPSIN was investigated by UV-VIS spectrophotometer and spectrophlorimetry. Spectral measurements were made by sodium phosphate buffer (.02M) at pH: 2 and temperatures between 30 and 100oC. It was observed that 1. High considerable enzyme stability, 2. Enzyme stability decreases in the presence of urea at pH: 2. 3. Thermodynamic parameters decline in the presence of urea. 4. Florescence intensity increase in the presence of urea.

Background: Garlic (Allium sativum) is widely used as an additive in pickles around the world and particularly in Iran. Considering Garlic treatment function this study was conducted to survey the effect of this plant entrant on the secretion rate of acid and PEPSIN in the stomach.Materials and Methods: This study involves two groups of 12 rats (Control group and Garlic group). Animals were gone under anesthesia by nesdonal with 50 mg/kg JP and undertook surgical process, tracheotomy, laparatomy and gasteroadeodenostomy. Garlic extract 100 mg/kg was administered by gasterodeodenostomy canola. Tnyostric secretions, obtained in wash out way, 15 and 30 minutes after stress acid and PEPSIN were measured by Tetrameter and Anson aprooch, respectively.Results: The amount of acid in both bases was significantly increased in the garlic group compared to the control group (p<0.001). not significantly change was observed in PEPSIN secretion. The elevation of acid secretion had no significant relevance with sex.Conclusion: Garlic (Allium sativum) increases acid secretion when used in food regimen.

Background and Aim: Antimicrobial peptides have attracted significant attention in recent decades because of their properties, such as rapid bactericidal effects, having a wide spectrum of activity, and a rare development of drug resistance. The purpose of this study was to examine the antibacterial activity of a peptide derived from the lactoferrin isolated from camel milk against Staphylococcus aureus, Pseudomonas aeruginosa, and Acinetobacter baumannii. Materials and Methods: In the present study, by means of bioinformatics, an antibacterial peptide was potentially identified as candidates in lactoferrin of camel milk, and an appropriate peptide was selected based on defined criteria. The PEPSIN-Camel-Lac1 peptide was synthesized. The methyl thiazolyl diphenyl-tetrazolium bromide assay was conducted to examine the toxicity of PEPSIN-Camel-Lac1 against a cell line. Three pathogenic bacteria, namely S. aureus, P. aeruginosa, and A. baumannii were analyzed to assess the antibacterial activity of PEPSIN-Camel-Lac1 peptide. Results: The results showed that the newly-identified peptide had no toxicity against the cell line. The minimum inhibitory concentration values of PEPSIN-Camel-Lac1 against S. aureus, P. aeruginosa, and A. baumannii were 31. 25 μ g/mL, 31. 25 μ g/mL, and 62. 5 μ g/mL, respectively. Conclusion: It seems that the growth of S. aureus, P. aeruginosa, and A. baumannii was not affected by PEPSIN-Camel-Lac1 treatment in the bacterial culture medium.

Porcine PEPSIN A (EC 3.4.23.1), belongs to the aspartic protease family, and is secreted as a zymogen called PEPSINogen. PEPSINogen activation occurs at pH values between 1 and 4. PEPSIN consists of a bilobal conformation with two catalytic aspartic residues (Asp32 and Asp215) on either side of the active site, The structure of porcine PEPSIN is predominantly b-strand and random coil with limited a-helix. Porcine PEPSIN is most efficient cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine. Because the importance of PEPSIN enzyme as an industrial enzyme in the food industry and nano particles functions in industry, we investigated Structural stability of PEPSIN in presence and absence of ZnO and Fe3O4 nanoparticles. This study were performed using glycin-Hcl (0.1M) buffer at pH=2 and temperature range (303 to 363) K. porcine PEPSIN stability Was not changed in the presence of Zno and Fe3O4 nanoparticles. Strength of the electrostatic and hydrogen interactions between PEPSIN enzyme and ZnO, Fe3O4 nanoparticles Were a low level in denaturation of PEPSIN.

Background and Objectives: In recent years, there has been a growing interest to identify bioactive peptides from plant sources. Enzymatic hydrolysis of proteins is the most common method to produce bioactive peptides. Wheat germ is one of the most important by-products from flour processing industry that it is rich in protein and amino acids composition. In this study, it was used as a valuable protein source to produce antioxidant peptide. Materials & Methods: Enzymatic hydrolysis of wheat germ was done by PEPSIN. The hydrolysis parameters were optimized in production of wheat germ protein hydrolysates with the highest antioxidant activity using response surface methodology. Then the hydrolysates obtained under optimized conditions were fractionated by RP-HPLC and fraction that exhibited the highest ABTS radical scavenging was identified by nano-LC/MS/MS proteomics. Results: The mathematical model presented a plateau region with maximum antioxidant activity at the following critical values: temperature = 37􀀀 C, time = 270 min and E/S ratio=1. 58%. The results of sequencing showed that the purified peptide had the sequence of KELPPSDADW with the molecular weight of 1157. 54 Da. This peptide had scavenging activity against DPPH (51± 1. 4%) and ABTS (86± 1. 1%) Conclusion: The results indicated that the peptide KELPPSDADW isolated from wheat germ protein has a strong antioxidant activity.