Asset Details
Do you wish to reserve the book?
Antioxidant and sensory properties of protein hydrolysate derived from Nile tilapia (Oreochromis niloticus) by one- and two-step hydrolysis
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Antioxidant and sensory properties of protein hydrolysate derived from Nile tilapia (Oreochromis niloticus) by one- and two-step hydrolysis
Do you wish to request the book?
Antioxidant and sensory properties of protein hydrolysate derived from Nile tilapia (Oreochromis niloticus) by one- and two-step hydrolysis
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Antioxidant and sensory properties of protein hydrolysate derived from Nile tilapia (Oreochromis niloticus) by one- and two-step hydrolysis
2015
Overview
Antioxidant and sensory properties of Nile tilapia protein hydrolysates prepared by one- and two-step hydrolysis using commercial proteases were investigated. Hydrolysates prepared using single protease including Alcalase (HA), Flavourzyme (HF), Protamex (HPr) and papain (HPa) had increases in antioxidant activities as the degree of hydrolysis (DH) increased up to 40 % (
P
< 0.05). Amongst all hydrolysates, HA having 40 % DH showed the highest antioxidant activities. When HA was further hydrolysed by papain, the resulting hydrolysate (HAPa) exhibited the highest antioxidant activities for all assays tested (
P
< 0.05). ABTS radical scavenging activity and metal chelating of HAPa generally remained constant in a wide pH range (1–11) and during heating at 30–100 °C. Both activities increased in the simulated gastrointestinal tract model system, especially in intestine condition. HAPa (100–1,000 ppm) could retard lipid oxidation in β-carotene-linoleate and lecithin-liposome model systems in a dose dependent manner. Peptides in both HA and HAPa with molecular weight of 513 Da and 1,484 Da possessed the strongest ABTS radical scavenging activity and metal chelating activity, respectively. The amino acid profile of both HA and HAPa contained a high amount of hydrophobic amino acids (38.26–38.85 %) and had glutamic acid/glutamine, lysine and aspartic acid/asparagine as the dominant amino acids. However, HAPa showed a higher acceptability than did HA, owing to the lower bitterness. Therefore, the use of Alcalase in combination with papain for hydrolysis of protein isolate rendered the hydrolysate with antioxidant properties and reduced bitterness, which could serve as the functional supplement.
