Antioxidant and functional properties of protein hydrolysates obtained from squid pen chitosan extraction effluent. (15th July 2017)

• Record Type: Journal Article
• Authors: Shavandi, Amin; Hu, Zhihao; Teh, SueSiang; Zhao, Jenny; Carne, Alan; Bekhit, Adnan; Bekhit, Alaa El-Din A.
• Is Part Of: Food chemistry. Volume 227(2017)
• Page Start: 194
• Page End: 201
• Publication Date: 2017-07-15
• Subjects: Squid pen -- Alkali hydrolysis -- Protein hydrolysis -- Bioactive peptides; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2017.01.099
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Squid pen protein from wastewater was hydrolysed by trypsin, pepsin and a bacterial protease called HT. Trypsin and HT hydrolysates generated more antioxidant activity than pepsin hydrolysates. High ACE-inhibitory activity was generated in the trypsin and pepsin hydrolysates. Protein recovered from chitosan processing waste solution can be a potential source of biopeptides. 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 24 h. 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).