Effect of sonication pretreatment parameters and their optimization on the antioxidant activity of Hermitia illucens larvae meal protein hydrolysates
Journal of Food Processing and Preservation • 2019
Publication Information
Authors
Benjamin Kumah Mintah; Ronghai He; Mokhtar Dabbour;
Moses Kwaku Golly; Akwasi Akomeah Agyekum; Haile Ma
Keywords
Not Available
Journal
Journal of Food Processing and Preservation
Publisher
Wiley
Volume
43
Issue
9
Pages
e14093
publication.type
International
Paper Link
Open Link
Supplementary Materials
Not Available
Abstract
The study investigated the effect of sonication conditions on antioxidant activity
of Hermetia illucens larvae meal protein hydrolysates. Three‐factor three‐level: pH
(7–9), time (10–30 min), and temperature (25–55°C) were optimized. Box–Behnken's
design was applied to optimize sonication treatment. Ferrous ion chelating activity
(ICA), DPPH‐radical scavenging activity (DPPHRSA), Hydroxyl radical scavenging activity
(HRSA), and cupric ion chelating activity (CCA) were considered as responses.
Findings demonstrated that sonication preceding enzymolysis significantly impacted
on ICA, DPPHRSA, HRSA, and CCA. ANOVA showed the determination coefficient
(R2) were 0.98 (ICA), 0.99 (DPPHRSA), 0.98 (HRSA), and 0.88 (CCA); demonstrating
that the models were reasonably fit with experimental results. Optimum sonication
conditions were pH (9), time (29.84 min), and temperature (54.93°C). For these conditions,
the experimental data obtained [ICA (37.84%), DPPHRSA (43.19%), HRSA
(71.01%), and CCA (68.93%)] were consistent with predicted values, higher than control,
and supported by protein subunits, fluorescence spectra and microstructure.
of Hermetia illucens larvae meal protein hydrolysates. Three‐factor three‐level: pH
(7–9), time (10–30 min), and temperature (25–55°C) were optimized. Box–Behnken's
design was applied to optimize sonication treatment. Ferrous ion chelating activity
(ICA), DPPH‐radical scavenging activity (DPPHRSA), Hydroxyl radical scavenging activity
(HRSA), and cupric ion chelating activity (CCA) were considered as responses.
Findings demonstrated that sonication preceding enzymolysis significantly impacted
on ICA, DPPHRSA, HRSA, and CCA. ANOVA showed the determination coefficient
(R2) were 0.98 (ICA), 0.99 (DPPHRSA), 0.98 (HRSA), and 0.88 (CCA); demonstrating
that the models were reasonably fit with experimental results. Optimum sonication
conditions were pH (9), time (29.84 min), and temperature (54.93°C). For these conditions,
the experimental data obtained [ICA (37.84%), DPPHRSA (43.19%), HRSA
(71.01%), and CCA (68.93%)] were consistent with predicted values, higher than control,
and supported by protein subunits, fluorescence spectra and microstructure.
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