Preparation and evaluation of antioxidant peptide from papain hydrolysate of?Sphyrna lewini muscle protein

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• 作者：Hong-Yu Luo^a ; ^b ; ^{hyluo11@hotmail.com} ; Bin Wang^a ; ^{wangbin4159@hotmail.com} ; Zhong-Rui Li^a ; Chang-Feng Chi^a ; Qi-Hong Zhang^a ; Guang-yuan He^b
• 关键词：Sphyrna lewini ; Hydrolysate ; Antioxidant activity ; Peptide
• 刊名：Lebensmittel-Wissenschaft und -Technologie
• 出版年：2013
• 出版时间：April, 2013
• 年：2013
• 卷：51
• 期：1
• 页码：281-288
• 全文大小：437 K

文摘

Inspired by DPPH radical scavenging assay, an efficient method had been developed to acquire the hydrolysate from Sphyrna lewini muscle protein (SPH) by an orthogonal L₉(3)⁴ test. Under optimal proteolysis parameters (proteolysis time 2?h, total enzyme dose 1.2 % , proteolysis temperature 60?¡ãC and pH 6), DPPH radical scavenging rate of SPH reached to 91.27?¡À?2.69 % at the concentration of 25?mg/mL. Proteolysis time showed significant effects on hydrolysate preparation (p?<?0.05). One peptide (SAP) was isolated from SPH by using ultrafiltration, anion-exchange chromatography, gel filtration chromatography and Reversed Phase High Performance Liquid Chromatography (RP-HPLC). The primary structure of SAP was identified as Leu-Asp-Lys with molecular weight of 374.44?Da. SAP exhibited good scavenging activity on hydroxyl radical (EC₅₀ 0.17?mg/mL), ABTS radical (EC₅₀ 0.19?mg/mL), and superoxide anion radical (EC₅₀ 0.12?mg/mL), but moderate DPPH radical (EC₅₀ 3.06?mg/mL). SAP was also effective against lipid peroxidation in the model system and peroxyl free radical scavenging in ¦Â-carotene linoleic acid assay. These results suggested that SAP could be used as natural antioxidant in enhancing antioxidant properties of functional foods and in preventing oxidation reactions in food processing.