Volume 14 Issue 6
Dec.  2018
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QIU Chaoying, RONG Jing, HU Xiao, YANG Xianqing, LI Laihao, HUANG Hui. Antioxidant properties of simulated in vitro digests of glycosylated Symplectoteuthis oualaniensis myofibrillar protein[J]. South China Fisheries Science, 2018, 14(6): 105-112. DOI: 10.12131/20180074
Citation: QIU Chaoying, RONG Jing, HU Xiao, YANG Xianqing, LI Laihao, HUANG Hui. Antioxidant properties of simulated in vitro digests of glycosylated Symplectoteuthis oualaniensis myofibrillar protein[J]. South China Fisheries Science, 2018, 14(6): 105-112. DOI: 10.12131/20180074
shu

Antioxidant properties of simulated in vitro digests of glycosylated Symplectoteuthis oualaniensis myofibrillar protein

  • 1.

    Key Laboratory of Aquatic Product Processing, Ministry of Agriculture and Rural Affairs; National R & D Center for Aquatic Product Processing; South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China

  • 2.

    Department of Food Science and Engineering, Jinan University, Guangzhou 510632, China

  • 3.

    College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China

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  • Received Date: April 22, 2018
  • Revised Date: June 06, 2018
  • Available Online: December 05, 2018
    Graphical Abstract
    • Abstract
  • The myofibrillar proteins extracted from purple back flying squids (Symplectoteuthis oualaniensis) were glycosylated with alginate oligosaccharide, and the glycosylated protein was simulated in vitro hydrolyzed by pepsin and pancreatin. The antioxidant properties and amino acids contents were analyzed. Results show that the free amino acids concentration decreased significantly after glycosylation, which was more obvious for the first 12 h, indicating the reaction occurred between protein and saccharides. The free radical DPPH and reducing power of both protein and the in vitro digests increased after glycosylation greatly (P<0.05). Therefore, the glycosylation increased the antioxidant properties of protein. While the radical scavenging ability and reducing power decreased after hydrolysis. The SDS-PAGE indicates that glycosylated protein showed bands with greater molecule weight, and its hydrolysates had more peptides with lighter molecule weight, which suggests that the glycosylation process promoted protein hydrolysis. The essential amino acids contents decreased while hydrophobic amino acids contents increased for the glycosylated protein hydrolysates.
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