XLXu Luo

Xu Luo

*This is an algorithmically generated author record based on publicly available information.

Current Organizations / Institutes

The organizations/institutes from the scholar's latest article


Xu Luo has a total of 7 co-authors. Here are the top co-authors by number of shared publications:

  • Chuanyan Pan

    Engineering Research Center of Processing & Storage of Characteristic and Advantage Aquatic Products from Guangxi Guangxi Academy of Fishery Science Nanning China

    1 shared publication
  • Ermeng Yu

    Guangxi Key Laboratory of Marine Environmental Science, Guangxi Academy of Marine Sciences, Guangxi Academy of Sciences, Nanning 530007, China

    1 shared publication
  • Huawei Ma

    Guangxi Academy of Fishery Sciences

    1 shared publication
  • Min Lv

    Guangxi Enginerring Research Center of Processing & Storage of Aquatic Products, Guangxi Academy of Fishery Sciences, Nanning 530021, Guangxi, China

    1 shared publication
  • Qiufeng Ruan

    Guangxi Key Laboratory of Aquatic Genetic Breeding and Healthy Aquaculture, Guangxi Academy of Fishery Sciences, Nanning 530021, China

    1 shared publication
  • Rong Zhang

    Liunan District Modern Agricultural Industry Service Center of Liuzhou City, Liuzhou, Guangxi, China

    1 shared publication

Latest Publications

  • Open Access

    Influences of Trypsin Pretreatment on the Structures, Composition, and Functional Characteristics of Skin Gelatin of Tilapia, Grass Carp, and Sea Perch

    by Qiufeng Ruan, Weijie Chen, Min Lv, Rong Zhang, Xu Luo, Ermeng Yu, Chuanyan Pan, Huawei Ma

    Fish skin gelatin is an important functional product in the food, cosmetics, and biomedicine industries, and establishing a green and effective fish skin gelatin extraction method is an effective way to obtain high-quality gelatin and improve its production efficiency. In this study, a trypsin method was used to extract the skin gelatin of sea perch, tilapia, and grass carp, and the microstructures of skin gelatin of these three fish species were analyzed, with such functional characteristics as thermal stability, gel strength, and emulsifying properties measured. The study results show that the skin gelatin of sea perch and tilapia obtained through the trypsin method has a relatively big molecular mass, a dense network structure, and a stable trihelix conformation. In addition, the skin gelatin of these three fish species has a relatively high β-turn content in the secondary structure, good gel strength, and water absorption properties. The compositions of the collagen-associated proteins in the skin gelatins of these three fish species extracted with the trypsin method are significantly different from each other, with positive effects of decorin and biglycan on the stability of the network structure of gelatin and a certain damaging effect of metalloendopeptidase on the network structure of gelatin. The skin gelatin of tilapia has high thermal stability and good emulsifying performance. Therefore, this gelatin type has bright application prospects in such fields as food processing, cosmetics, and drug development. In contrast, the skin gelatin of grass carp has poor functional properties. Therefore, there are significant differences among the structures and functions of skin gelatin extracted from different kinds of fish through the trypsin method. This finding has provided a useful reference for the production of customized fish gelatin according to demand.