Published 2022

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Publication details

Journal : Food Chemistry , vol. 382 , p. 9 , 2022

Publisher : Elsevier

International Standard Numbers :
Printed : 0308-8146
Electronic : 1873-7072

Publication type : Academic article

Contributors : Kristoffersen, Kenneth Aase; Afseth, Nils Kristian; Böcker, Ulrike; Dankel, Elin Katinka Riiser; Pettersen, Mats Rønningen; Lislelid, Andreas; Ofstad, Ragni; Lindberg, Diana; Wubshet, Sileshi Gizachew

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Enzymatic protein hydrolysis (EPH) is an invaluable process to increase the value of food processing by-products. In the current work the aim was to study the role of standard thermal inactivation in collagen solubilization during EPH of poultry by-products. Hundred and eighty hydrolysates were produced using two proteases (stem Bromelain and Endocut-02) and two collagen-rich poultry by-products (turkey tendons and carcasses). Thermal inactivation was performed with and without the sediment to study the effect of heat on collagen solubilization. A large difference in molecular weight distribution profiles was observed when comparing hydrolysate time series of the two proteases. In addition, it was shown that 15 min heat treatment, conventionally used for inactivating proteases, is essential in solubilizing collagen fragments, which significantly contributes to increasing the protein yield of the entire process. The study thus demonstrated the possibility of producing tailored products of different quality by exploiting standard heat inactivation in EPH.


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