Affiliations 

  • 1 Department of Food Science, University of Otago, Dunedin, New Zealand. Electronic address: Amin.shavandi@otago.ac.nz
  • 2 Department of Food Science, University of Otago, Dunedin, New Zealand
  • 3 Department of Bioscience and Sport Science, Faculty of Applied Sciences and Computing, Tunku Abdul Rahman University College, Jalan Genting Kelang, 53300 Kuala Lumpur, Malaysia
  • 4 Faculty of Agriculture and Life Sciences Lincoln University, Lincoln Canterbury, New Zealand
  • 5 Department of Biochemistry, University of Otago, Dunedin, New Zealand
  • 6 Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Alexandria University, Alexandria, Egypt
  • 7 Department of Food Science, University of Otago, Dunedin, New Zealand. Electronic address: Aladin.bekhit@otago.ac.nz
Food Chem, 2017 Jul 15;227:194-201.
PMID: 28274422 DOI: 10.1016/j.foodchem.2017.01.099

Abstract

Squid pens were subjected to alkali hydrolysis to extract chitin and chitosan. Proteins present in the alkaline extraction wastewater were recovered at pH 3, 4, 5 and 6, and were subjected to hydrolysis by trypsin, pepsin and a bacterial protease called HT for 1, 2, 4 and 24h. Hydrolysis of the extracted proteins with either trypsin or HT generated more antioxidant activity than hydrolysis with pepsin. Higher ACE-inhibitory activity was generated in the trypsin and pepsin hydrolysates than in the HT hydrolysate. Squid pen protein recovered from chitosan processing waste alkaline solution can be a potential source of bioactive peptides for addition to foods. The antioxidant and ACE-inhibitory activities of the extracted proteins were initially low and increased upon incubation with the proteases. Pepsin generated significantly lower (P<0.05) antioxidant activities compared to trypsin and HT, while trypsin and pepsin hydrolysates exhibited higher ACE-inhibitory activity than HT (P<0.05).

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.