Share
استخلاص وتنقية وتوصيف متحللات بروتينية من مخلفات الاسماك والروبيان واختبار كفاءتها في حفظ اقراص مفروم اللحم البقري == Extraction, purification and Characterization of Protein hydrolysates From Fish and Shrimp by - Products and Assay Efficiency in Beef Patties Storage
Author name:
عالية زيارة هاشم الحلفي
Supervisor name:
ام البشر حميد جابر الموسوي
General topic:
Agricultural sciences
Specific topic:
Food
Degree:
Doctorate
University:
University Of Basrah - Faculty Of Agriculture
Language:
Arabic
University location:
Basrah
First pages:
31T1822 - p.pdf
Abstract:
The study was interested in the preparation of bioactive peptides by using shrimp and fish by products.Three types of proteolytic enzymes , Alcalase and Pepsin and Flavourzyme were used for this purpose.The constituents (moisture , protein , fat and ash) of defatted raw and dried materials were studed .The proteolysis action of the three enzymes was observed for 5 hours the peptides chain length of the protein hydrolysates were determined and tested for their antioxidat and antibacterial 240 minutes of enzyme assay was reliance according to the highly antioxidantive and antibacterial properties of produced peptides.The proteolysis of shrimp by - product by Alcalase and Pepsin gave highly antioxidantive activity. The isolation , purification and the peptides bioactivity determination was achieved as below : 1 - The peptides of the both protein hydrolysates were isolated by using Ultrafiltration membranes of 5 MWCO KDa. The isolated peptides were examined for their antioxidative activity. It shown , that the peptides wjich was synthesized by the proteolytic activity of Alcalase has ahigher antioxidative action (53.67%) comparing with pepsin peptides (41.19%) at concentration of 100 mg/mL. The results showed that peptides of hydrolysate enzyme Pepsin give inhibitor zoon against bacteria test in inhibition zoon ranged from 10 - 11 mm and determined peptides content of amino acids and showed glysin , threonine ,valine and lysine, which amounted to 9.11% and 8.94% and 7.51% and 9.16%, respectively in peptides of enzyme Alcalase while recorded amino acids serine 9.69% ,theronine 8.76% ,cystin 14.10% and 7.06% lysine ratios highest peptides hydrolysate enzyme Pepsin respectively.Summaryb2 - purification of peptides by gel filtration was showed four peaks of peptides hydrolysate enzyme Alcalase and three peaks for peptides hydrolysate Pepsin enzyme and tested the antioxidation activity of all peaks and inhibitory to bacteria, which recorded that second peak of the Alcalase enzyme antioxidant activity amounted to 63.28% and peptides The first peak of the same enzyme%48.57 the peptides first and the second peak for hydrolysate Pepsin enzyme was% 41.65 and 55.21% also tested the inhibitory effect against some types of bacteria have been to peptides second peak of the Pepsin enzyme hydrolysate towards the bacteria Escherichia coli, Salmonella typhi, Staphylococcus aureus, Bacillus cereus , Pseudomonas aeruginosa inhibition zoon ranged 13 - 9 mm, and determined the minimum inhibitory concentrations (MIC) of these peptides and found that the concentration of 125 and 250 mg / ml values have affected all types of bacteria testing. The cellular toxicity of peptide peakes in analysis of human red blood cells, and has not any toxic effect observed for all concentrations and different periods incubation of peptides peasks.3 - The molecular weight of peptides two of peak enzymes was determined by electrophoresis and cleared two bandes each peak represents two chain peptide molecular weights 3.71 and 4.37 KDa the first peak and the second peak 3.71 and 4.27 KDa of the hydrolysate Alcalase enzyme and chains peptides first peak of hydrolysate Pepsin enzyme 3.71 and 4.16 KDa the second peak, 3.71 and 3.98 KDa, respectively , The study included determined of amino acids and found that it contains all the amino acid varying percentages depending on peptides peakes hydrolysate protein.4 - The stability of antioxidant peptides towards thermal treatment to different degrees thermal ranged between 25 - 100C and change in pH 2 - 11 and treatment of sodium chloride salt ranged between %2 - 8 was studed and found that the antioxidant activity of peptides and reducing power stable at 60C The ability to binding ion ferrous ,hydrogen peroxide , hydroxyl radical scavenging and superoxide anion scavenging they appear stable at thermal 40C and whenctesting the stability of peptides to change the pH was observed that the peptides two peakes hydrolysate enzyme Alcalase stable at pH 8 but decreases when moving away from this value towards the basic or acidic while shwoed peptides two peakes hydrolysate enzyme Pepsin stability at pH 7, and this stability declined when number pH to 11, and when the treatment with salt sodium chloride showed peptides first peak and second enzyme Alcalase and Pepsin stable antioxidant activity at 4% salt concentration for all tests except the oxidation stability of peptides in binding ferrous ion has showed at 6% salt concentration.5 - when the follow of peroxide values for beef patties treated with peptides two peakes enzymes, The results showed there is adecrease in peroxide values for beef patties treated with peptides of the Alcalase enzyme was more cleared compared to the peptides of first peak for the same enzyme and peptides two peakes Pepsin enzyme also got a decrease in the total number of bacteria and total coliform bacteria and psychrophilic bacteria When the treatment second peptides peak of the Pepsin enzyme concentration of 50 and 100 mg / 100 g meat.6 - Sensory evaluation of beef patties showed that the treatment samples with peptides second peak of the Alcalase enzyme recorded the highest degree of sensory evaluation peptides compared with the first peak of the same enzyme and peptides peaks hydrolysate Pepsin enzyme.
