TY - JOUR
T1 - Effects of pressure-assisted enzymatic hydrolysis on functional and bioactive properties of tilapia (Oreochromis niloticus) by-product protein hydrolysates
AU - Hemker, Ashutosh Kumar
AU - Nguyen, Loc Thai
AU - Karwe, Mukund
AU - Salvi, Deepti
N1 - Funding Information:
This project was supported by the Global Advancement and International Affairs (GAIA) International Collaborative Research Grants award of Rutgers, The State University of New Jersey, USA. The authors are also thankful to Washington State University, USA for facilitating the high-pressure processing of protein samples. The author would also like to acknowledge help from Sawali Naware in high-pressure processing of protein samples.
Funding Information:
This project was supported by the Global Advancement and International Affairs (GAIA) International Collaborative Research Grants award of Rutgers, The State University of New Jersey, USA . The authors are also thankful to Washington State University, USA for facilitating the high-pressure processing of protein samples. The author would also like to acknowledge help from Sawali Naware in high-pressure processing of protein samples.
Publisher Copyright:
© 2020 Elsevier Ltd
PY - 2020/3
Y1 - 2020/3
N2 - Fish by-product protein can be converted into valuable food and nutraceutical ingredients via proteolysis. The existing process suffers from many limitations such as extended reaction time and nonselective hydrolysis. In this study, protein from tilapia fish by-products was transformed into functional peptides using pressure-assisted enzymatic hydrolysis. Proteins were extracted from the tilapia by-products by isoelectric solubilization and precipitation method. The effects of pressure (38–462 MPa) and hydrolysis time (6–35 min) on the properties of the hydrolysates were investigated using a central composite design. Pressure enhanced protein hydrolysis with a maximum trichloroacetic acid-solubility index (TCA-SI) of 23% obtained at 250 MPa for 35 min. Pressure and time were also vital in improving soluble protein content (5.7 mg/mL), reducing power (44 μg AAE/g), and solubility (71%) of the hydrolyzed products. Improved antioxidant activity, indicated by a significant decrease in IC50 values from 653 μg/mL to 304 μg/mL, was recorded. The combined process facilitated the release of low-molecular-weight peptides and essential amino acids. However, water and oil holding capacities were found to be decreased. Pressure-assisted enzymatic hydrolysis could provide an effective approach for recovering bioactive peptides from fish by-products for industrial applications.
AB - Fish by-product protein can be converted into valuable food and nutraceutical ingredients via proteolysis. The existing process suffers from many limitations such as extended reaction time and nonselective hydrolysis. In this study, protein from tilapia fish by-products was transformed into functional peptides using pressure-assisted enzymatic hydrolysis. Proteins were extracted from the tilapia by-products by isoelectric solubilization and precipitation method. The effects of pressure (38–462 MPa) and hydrolysis time (6–35 min) on the properties of the hydrolysates were investigated using a central composite design. Pressure enhanced protein hydrolysis with a maximum trichloroacetic acid-solubility index (TCA-SI) of 23% obtained at 250 MPa for 35 min. Pressure and time were also vital in improving soluble protein content (5.7 mg/mL), reducing power (44 μg AAE/g), and solubility (71%) of the hydrolyzed products. Improved antioxidant activity, indicated by a significant decrease in IC50 values from 653 μg/mL to 304 μg/mL, was recorded. The combined process facilitated the release of low-molecular-weight peptides and essential amino acids. However, water and oil holding capacities were found to be decreased. Pressure-assisted enzymatic hydrolysis could provide an effective approach for recovering bioactive peptides from fish by-products for industrial applications.
KW - Fish by-products
KW - High-pressure processing
KW - Physicochemical properties
KW - Protein hydrolysis
KW - Response surface methodology (RSM)
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U2 - 10.1016/j.lwt.2019.109003
DO - 10.1016/j.lwt.2019.109003
M3 - Article
AN - SCOPUS:85078247490
SN - 0023-6438
VL - 122
JO - LWT
JF - LWT
M1 - 109003
ER -