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The Influence of the Extent of Enzymatic Hydrolysis on Antioxidative Properties and ACE-Inhibitory Activities of Protein Hydrolysates from Goby (Zosterisessor ophiocephalus) Muscle

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Abstract

Antioxidant properties and angiotensin-converting enzyme (ACE) inhibitory activities of protein hydrolysates from goby (Zosterisessor ophiocephalus) muscle, with different degrees of hydrolysis (DH) from 5 to 25 %, prepared by treatment with crude proteases extract from smooth hound intestines, were investigated. Goby protein hydrolysates (GPHs) are rich in Gly and Thr, which accounted for 14.1–15 % and 11.6–13.2 % of the total amino acids, respectively. The antioxidant activities of GPHs were investigated by using several in vitro assay systems. All GPHs exhibited significant metal chelating activity and DPPH free radical-scavenging activity, and inhibited linoleic acid peroxidation. For the ACE-inhibitory activity, as the DH increased, the activity of GPHs increased. The obtained results revealed that antioxidant and ACE-inhibitory activities of GPHs were influenced by the degree of hydrolysis. A medium degree of enzymatic hydrolysis was appropriate to obtain GPHs with good antioxidant activity, while small peptides were essential to obtain high ACE inhibitory activity.

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Acknowledgments

This work was funded by the Ministry of Higher Education and Scientific Research, Tunisia.

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Correspondence to Rim Nasri.

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Nasri, R., Jridi, M., Lassoued, I. et al. The Influence of the Extent of Enzymatic Hydrolysis on Antioxidative Properties and ACE-Inhibitory Activities of Protein Hydrolysates from Goby (Zosterisessor ophiocephalus) Muscle. Appl Biochem Biotechnol 173, 1121–1134 (2014). https://doi.org/10.1007/s12010-014-0905-3

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  • DOI: https://doi.org/10.1007/s12010-014-0905-3

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