食品SCI论文赏析.ppt

食品SCI论文赏析.pptPurification and characterization of antioxidant peptides from enzymatically hydrolyzed chicken egg white鸡蛋清蛋白酶解物中抗氧化多肽的纯化与特性描述
Name
Numember 2015872016

2. Materials and methods
3. Results and discussion
Highlights
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Chicken egg white was hydrolysed using several non-gastrointestinal proteases.
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Egg white hydrolysed by protease-P showed highest antioxidant activity.
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The hydrolysate was purified to isolate antioxidant peptides.
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Sixteen antioxidant peptides were purified and amino acid sequences were determined.
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Synthesized peptide AEERYP showed the highest antioxidant activity
重点
鸡蛋白是使用几个非肠胃蛋白酶水解。
经protease-P水解的蛋白显示最高的抗氧化活性。
水解产物的纯化分离是隔绝抗氧化肽

16个抗氧化肽经纯化并且氨基酸序列已被测定
合成肽AEERYP显示最高的抗氧化活性
Abstract
Egg white is considered as a rich source of high quality proteins with various bioactive peptide fractions. Enzymatic hydrolysis of proteins can be used to release bioactive fractions and different enzymes have different abilities in releasing such bioactive fractions depending on the enzyme’s site of activity on a protein. In this study, several proteases were examined for their ability to release antioxidant peptides from hen egg white and protease P was selected based on the antioxidant activity and the digestion yield of the crude protein hydrolysate. bination of several purification steps including ultrafiltration with low molecular weight cut-off membranes, cation exchange chromatography and reversed phase high performance liquid chromatography was used to purify ‘protease P egg white hydrolysate’. Sixteen antioxidant peptides, which were derived from ovalbumin, ovotransferrin and cystatin were isolated from the most active fractions. Amino acid sequences of those peptides were determined using LC–MS/MS. Oxygen radical absorbance capacity (ORAC) values of selected short chain peptides were determined using synthetic peptides. Two peptides AEERYP and DEDTQAMP (Ala-Glu-Glu-Arg-Tyr-Pro and Asp-Glu-Asp-Thr-Gln-Ala-Met-Pro) showed the high