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. 2013 Feb 1;14(2):3124-39.
doi: 10.3390/ijms14023124.

Optimization of the preparation of fish protein anti-obesity hydrolysates using response surface methodology

Liyuan Liu  1 , Yanping Wang, Chen Peng, Jinju Wang
Affiliations

Optimization of the preparation of fish protein anti-obesity hydrolysates using response surface methodology

Liyuan Liu et al. Int J Mol Sci. .

Abstract

The enzymatic condition for producing the anti-obesity hydrolysates from fish water-soluble protein was optimized with the aid of response surface methodology, which also derived a statistical model for experimental validation. Compared with neutral protease, papain and protamex, the porcine pancreas lipase inhibitory rate of hydrolysates from fish water-soluble protein was higher with alkaline protease. Results showed that the model terms were significant, the terms of lack of fit were not significant, and the optimal conditions for the hydrolysis by alkaline protease were initial pH 11, temperature 39 °C, enzyme dosage 122 U/mL and 10 h of hydrolysis time. Under these conditions, the porcine pancreas lipase and the α-amylase inhibitory rate could reach 53.04% ± 1.32% and 20.03 ± 0.89%, while predicted value were 54.63% ± 1.75%, 21.22% ± 0.70%, respectively. In addition, Lineweaver-Burk plots showed noncompetitive inhibition. The K(i) value calculated was 84.13 mg/mL. These results demonstrated that fish water-soluble protein could be used for obtaining anti-obesity hydrolysates.

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Figures

Figure 1
Figure 1
Degree of hydrolysis (a) and porcine pancreas lipase (PPL) inhibitory rate (b) during different stages of enzymatic hydrolysis using four proteases. The error bars represent standard deviations from three independent samples.
Figure 2
Figure 2
Response surface plots and contour plots for the interactive effects of variables on the porcine pancreas lipase (PPL) inhibitory rate. (a) the interactive effects of initial pH and temperature, maintaining fixed enzyme dosage 100 U/mL, hydrolysis time 10 h; (b) the interactive effects of initial pH and hydrolysis time, maintaining fixed enzyme dosage 100 U/mL, temperature 45 °C; (c) the interactive effects of temperature and hydrolysis time, maintaining fixed enzyme dosage 100 U/mL, initial pH 11; (d) the interactive effects of enzyme dosage and hydrolysis time, maintaining fixed initial pH 11, temperature 45 °C.
Figure 3
Figure 3
Contour plots for the interactive effects of variables on the α-amylase inhibitory rate. (a) the interactive effects of hydrolysis time and temperature, maintaining fixed enzyme dosage 100 U/mL, initial pH 11; (b) the interactive effects of enzyme dosage and initial pH, maintaining fixed hydrolysis time 10 h, temperature 45 °C.
Figure 4
Figure 4
Fitted line plot indicating the closeness between predicted values and experimental values for porcine pancreas lipase (PPL) inhibitory rate (a) and α-amylase inhibitory rate (b).
Figure 5
Figure 5
Lineweaver-Burk plots for the inhibition of porcine pancreas lipase (PPL) by fish protein hydrolysates (FPH). The reactions were performed at a constant concentration [0 mg/mL (●), 60 mg/mL (■) and 90 mg/mL (▲)] of polypeptide in hydrolysates. Each bar showed the standard deviations. Values were the means of triplicate analyses.
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