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Study On The Preparation Of Collagen Of Deer Bone And Antioxidant Activity Of It's Hydrolysates

Posted on:2008-07-03Degree:MasterType:Thesis
Country:ChinaCandidate:T GaoFull Text:PDF
GTID:2144360215993761Subject:Food Science
Abstract/Summary:PDF Full Text Request
Chian is a major country of deer processing. Deer bone is one of the most plentiful byproducts in deer processing industry. In this study, the collagen of deer bone was hydrolyzed with proteinase to get antioxidative peptide.Acide-soluble collagen (ASC) and pepsin-solubilized collagen (PSC) were isolated from deer bone. The maximum absorption of ASC and PSC were 234nm and 230nm on ultraviolet spectrophotometry. By infrared spectrum we know that ASC and PSC have simiIar structure. The shrinkage temperature of ASC and PSC were 55℃and 58℃respectively. ASC and PSC are typicallyⅠcollagen.The gelatin of deer bone was extracted by hot water. The optimal conditions were found by single factor experiments and orthogonal tests, which was temperature 95℃, time 3h, ratio of decalcified deer bone to water 1:15. And the highest extration yield of deer bone gelatin was 67.9%.Deer bone gelatin was hydrolyzed with Alcalase, neutrase or trypsinase. Single factor experiment and orthogonal tests were adopted to find the optimal hydrolysis condition. That of Alcalase was temperature 65℃, pH 9.5, the amount of Alcalase 4500U/g. For neutrase or trypsinase, the optimal hydrolysis condition was temperature 50℃, pH 8.5, the amount of Alcalase 7000U/g.The gelatin hydrolysates prepared by Alcalase, neutrase or trypsinase exhibited the stronger power to arrest·OH and O2-radicals than nonhydrolyzed gelatin. Radical-scavenging activity increased with hydrolysis time. Alcalase-hydrolyzed gelatin had strongest power to arrest·OH and O2-radicals. Fe2+-chelating activity of hydrolysates was influenced by hydrolysis time and sorts of proteinase. On the whole, Fe2+-chelating activity increased with hydrolysis time. The gelatin hydrolysates of Alcalase had strongest Fe2+-chelating activity. And Fe2+chelating activity Of nonhydrolyzed gelatin was largely lower than both hydrolysates. The hydrolysates exhibited significant inhibition of lipid peroxide formation. However, Alcalasehydrolyzed gelatin exhibited stronger antioxidant activity at any of the hydrolysis time. Nonhydrolyzed gelatin showed slight inhibitory effect on lipid oxidation, lower than hydrolysates heavily. The hydrolysates of deer bone gelatin can work as a radical stabilizer and metal ion chelator to inhibit lipid oxidation.At last, hydrolysates had better solubility and hygroscopicity than gelatin. And gelatin has better Moisture retention than hydrolysates.The study showed that hydrolysates of Alcalase can inhibit oxidation of soybean oil and olive oil. The antioxidant activity increased with the amount of hydrolysates. Antioxidant containing hydrolysates and VE showed stronger antioxidant activity than single antioxidant.
Keywords/Search Tags:Deer bone, collagen, hydrolysis, antioxidative peptide, functional properties
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