Determination of Functional Properties of Peptides Derived from Ovalbumin Using Protease Enzyme Under Different Conditions

Show simple item record

dc.contributor.author MADUSHANI, M.A.A.
dc.date.accessioned 2021-10-11T07:53:29Z
dc.date.available 2021-10-11T07:53:29Z
dc.date.issued 2013
dc.identifier.other UWU/ANS/13/0028
dc.identifier.uri http://www.erepo.lib.uwu.ac.lk/bitstream/handle/123456789/7222/ANS%2013%20028-17022021094730.pdf?sequence=1&isAllowed=y
dc.description.abstract Ovalbumin is the major and most abundant protein in chicken egg white. Ovalbumin hydrolysates (OVH) have high biological and nutritive value. Therefore, OVH are widely used in manufacturing of dietary supplements and functional food. Objective of this research was to compare the peptides produce from ovalbumin using protease enzyme with different temperature, time and pH condition and check its hydrolysates for its functional properties. Ovalbumin was dissolved with 20mg/m1 concentration and hydrolyzed using protease enzyme under different temperature conditions ranging from 37 °C to 50 °C, pH from 6.5-8.0 for 0-24 hrs. Level of hydrolyzing was observed with 15% SDS-PAGE gel electrophoresis system and visual observation. Best hydrolysates were subjected to functional properties using TBARS assay and DPPH Scavenging activity, antimicrobial assay, Fe2+ chelating activity and alpha amylase inhibitory activity. According to the TBARS assay, all OVH derived under different conditions show antioxidant property when compare with the oil emulsion (p<0.05). According to the DPPH assay, OVH which were produced showed some of scavenging activities under some conditions. OVH which was produced under 37 °C and pH 8 for 3hrs had the highest DPPH scavenging activity and was significant difference among the antioxidant properties observed (p<0.05). Concluding TBARS and DPPH values for the OVH which were derived under 37 °C and pH 8 for 3hrs conditions have good antioxidant property than the rest. However, all the OVH did not shoW good Fe2+ chelating activity. But there was a significant difference in Fe2+ chelating activity among the treatments (p <0.05) and trt12 showed highest chelating activity (11.19%±0.57) than the rest. According to the antimicrobial assay most of the OVH showed gbod antimicrobial property against Salmonella spp. and E. coli spp. And there was significant difference of antimicrobial property among the hydrolysates (p <0.05). OVH produced under 37 °C and pH 8 for 3hrs conditions showed highest antioxidant property and good antibacterial activity than the rest and it was the best condition to prepare OVH to having functional properties. However, applications of these peptides have to be further study for its applications in food industry. en_US
dc.language.iso en en_US
dc.publisher Uva Wellassa University of Sri Lanka en_US
dc.relation.ispartofseries ;UWU/ANS/13/0028
dc.subject Animal Science Degree Programme (ANS) en_US
dc.title Determination of Functional Properties of Peptides Derived from Ovalbumin Using Protease Enzyme Under Different Conditions en_US
dc.title.alternative Research Article – ANS 2013 en_US
dc.type Thesis en_US


Files in this item

This item appears in the following Collection(s)

Show simple item record

Search UWU eRepository


Browse

My Account