Abstract
The study aims at removal of lipid from ribbon fish protein hydrolysate (FPH) to enhance the protein content and analyse its physicochemical and bioactive properties. Ribbon fish protein hydrolysate was prepared using commercially available papain enzyme (1.5% w/v for 4 h). The resulting supernatant was further treated with lipase (0.5–2.0% w/v for 1–5 h). The treatment used in this study reduced ~ 98% of lipids depending on the enzyme concentration, temperature, pH, and duration of the treatment. Lipase treatment for 2 h increased the protein content from 62.87 to 94.11%. FPH after lipase treatment showed 1.21 folds increase in angiotensin-converting enzyme-I (ACE-I) inhibitory activity and 1.7 folds increase in standard amino acids composition (32.193 to 61.493 g/100 g). The physicochemical properties of FPH samples were analyzed by solubility, hygroscopicity, color, FT-IR, SEM, SDS-PAGE, and Zeta Potential. Use of lipase enzyme for separating the lipid content from protein hydrolysate without conferring any undesirable adverse effects on the physicochemical properties of protein hydrolysate. Lipid-free protein hydrolysates can be of commercial importance for their enhanced ACE-I inhibitory activity, replacing the side effect causing synthetic drugs for hypertension, and can have potential applications in developing functional food formulations.
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The data obtained in this study are available.
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Abbreviations
- FPH:
-
Fish protein hydrolysate
- DH%:
-
Degree of hydrolysis
- CFPH:
-
Control fish protein hydrolysate
- TFPH:
-
Test fish protein hydrolysate
- FT-IR:
-
Fourier transform infrared
- SEM:
-
Scanning electron microscopy
- HPLC:
-
High performance liquid chromatography
- RP-HPLC:
-
Reverse phase high performance liquid chromatography
- SDS-PAGE:
-
Sodium dodecyl sulfate polyacrylamide gel electrophoresis
- ACE:
-
Angiotensin converting enzyme
- HA:
-
Hippuric acid
- HHL:
-
N-Hippuryl-L-Histidyl-L-Leucine hydrate
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Acknowledgements
The authors are grateful to the Department of Science and Technology (DST) – Scientific Engineering Research Board (SERB), New Delhi, India for financial support through the project [No-YSS/2015/001301]. The authors thanks Prof. Dr. Anirban Chakraborty, The Director, Nitte University Centre for Science Education and Research (NUCSER). The authors extend their thanks to Prof. Dr. Indrani Karunasagar, The Director of projects, DST-NUTECH, Nitte University Centre for Science Education and Research (NUCSER) for her constant support.
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This work financially supported by Department of Science and Technology (DST) – Scientific Engineering Research Board (SERB), New Delhi, India, project [No-YSS/2015/001301].
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YUG: involved in planning and conducting the experiments, data compilation, statistical analysis of results and drafting the manuscript. MT: Assisting in conducting the experiments. IB: Involved in manuscript preparation. FL: Involve in review and editing of the manuscript. MBS: Corresponding author, contributed in planning and interpretation of the results, reviewing and finalization of the manuscript for publication.
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13197_2022_5620_MOESM2_ESM.jpg
Supplementary Fig. 1. Solubility (A) and hygroscopicity (B) of CFPH and TFPH. The values are mean ± SD from triplicate determinations (n = 3) and significant difference (p < 0.05) Note: CFPH- Control fish protein hydrolysate; TFPH- Test fish protein hydrolysate.
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Yathisha, U.G., Tanaaz, M., Bhat, I. et al. Physicochemical properties and angiotensin-I converting enzyme inhibitory activity of lipid-free ribbon fish (Lepturacanthus savala) protein hydrolysate. J Food Sci Technol 60, 340–352 (2023). https://doi.org/10.1007/s13197-022-05620-z
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DOI: https://doi.org/10.1007/s13197-022-05620-z