Acrylamide and 5-hydroxymethylfurfural (HMF) are potential compounds that are known to be neurotoxic, mutagenic, and carcinogenic when exposed to humans. These components are formed during Maillard reaction at which sugar is reduced and specific amino acids react at high temperature, and thus producing brown colour and flavour in food. Therefore, the aim of this study was to observe the formation level of acrylamide and HMF in fresh and frozen curry puff skins. This study investigated the effects of frozen storage and frying times on the formation of acrylamide and HMF in curry puff skin. Frozen curry puff skins were stored at -18°C for 0, 7, 14, and 28 days. The curry puff skins were fried at 180 °C for 2, 3, 5, and 7 min. Before that, the frozen curry puff skins were thawed at room temperature for 2 h. The changes in colour, moisture, and texture were measured as indicators to Maillard reaction. Frozen curry puff skins reduced the level of acrylamide and HMF to 70 % and 50 %, respectively after 28 days of storage. The colour development of frozen curry puff skins demonstrated less vividness as the storage time increased as compared to fresh curry puff skins. The fresh and frozen curry puff skins exhibited similar firmness and texture profile with no significant differences during the 4 weeks of storage.
The study aimed to investigate the molecular interaction of ACE-inhibitory peptides derived from collagen type I. Collagen type I alpha 1 and alpha 2 were used in this work was to analogue the tilapia by-product protein precursor for ACE-inhibitory peptides production. In silico production of ACE-inhibitory peptides derived collagen type I from BIOPEP was used to simulate peptide-ACE interaction using Autodock Vina. Most potent ACE-inhibitory tri-and di-peptides, Gly-Leu-Pro (GLP IC50 1.62 μM) and Cys-Phe (CF IC50 1.96 μM) derived alpha 1 and Leu-Gly-Pro (LGP IC50 0.72 μM), and Glu-Tyr (EY IC50 2.68 μM) derived alpha 2 were chosen from BIOPEP database. The hydrophobicity of the amino acids is suggested to contribute to bioactivity. These peptides inhibited the active sites of ACE at the C terminal residue. The zinc (II) interacted with all four peptides directly and indirectly. GLP and CY of alpha 1 could share a bond with His 383, His 387, and Glu 411 instead of directly binding to the zinc (II) atom. ACE has a zinc ion in its coordinates with His 383, His 387, and Glu 411. Alpha 2's LGP and EY were directly bound to Zinc (ii) atoms.
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