Current Organizations / Institutes

The organizations/institutes from the scholar's latest article


Chun Shing Lee has a total of 5 co-authors. Here are the top co-authors by number of shared publications:

  • Chee Fan Tan

    Bioprocessing Technology Institute (BTI), Agency for Science, Technology and Research (A*STAR), 20 Biopolis Way, Centros, Singapore 138668, Singapore

    1 shared publication
  • Soon Hong Kwan

    Bioprocessing Technology Institute (BTI), Agency for Science, Technology and Research (A*STAR), Singapore 138668, Singapore

    1 shared publication
  • Xuezhi Bi

    Bioprocessing Technology Institute (BTI), Agency for Science, Technology and Research (A*STAR), 20 Biopolis Way, #06-01 Centros, Singapore 138668, Singapore

    1 shared publication
  • Yan Ni Annie Soh

    Bioprocessing Technology Institute (BTI), Agency for Science, Technology and Research (A*STAR), Singapore 138668, Singapore

    1 shared publication
  • Ying Swan Ho

    Bioprocessing Technology Institute (BTI), Agency for Science, Technology and Research (A*STAR), Singapore, Republic of Singapore

    1 shared publication

Latest Publications

  • Open Access

    Cottonseed Meal Protein Isolate as a New Source of Alternative Proteins: A Proteomics Perspective

    by Chee Fan Tan, Soon Hong Kwan, Chun Shing Lee, Yan Ni Annie Soh, Ying Swan Ho, Xuezhi Bi

    Cottonseed meal (CSM) is a good source of dietary proteins but is unsuitable for human consumption due to its gossypol content. To unlock its potential, we developed a protein extraction process with a gossypol removal treatment to generate CSM protein isolate (CSMPI) with ultra-low gossypol content. This process successfully reduced the free and total gossypol content to 4.8 ppm and 147.2 ppm, respectively, far below the US FDA limit. In addition, the functional characterisation of CSMPI revealed a better oil absorption capacity and water solubility than pea protein isolate. Proteome profiling showed that the treatment improved protein identification, while SDS-PAGE analysis indicated that the treatment did not induce protein degradation. Amino acid analysis revealed that post-treated CSMPI was rich in branched-chain amino acids (BCAAs). Mass spectrometry analysis of various protein fractions obtained from an in vitro digestibility assay helped to establish the digestibility profile of CSM proteins. Several potential allergens in CSMPI were also found using allergenic prediction software, but further evaluation based on their digestibility profiles and literature reviews suggests that the likelihood of CSMPI allergenicity remains low. Overall, our results help to navigate and direct the application of CSMPIs as alternative proteins toward nutritive human food application.