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Steady-state kinetics of tryptic hydrolysis of β-lactoglobulin after dynamic high-pressure microfluidization treatment in relation to antigenicity

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Abstract

Our previous research revealed that dynamic high-pressure microfluidization (DHPM) increased the antigenicity of β-lactoglobulin (β-Lg) below 80 MPa, which was related to the unfolding of protein. To test the hypothesis that the unfolding of protein may change proteolytic susceptibility of β-Lg and modulate its antigenicity during the digestion, we developed that the steady-state kinetics of tryptic hydrolysis of β-Lg subjected to DHPM (0.1–80 MPa) have been investigated in relation to the antigenicity in this study. According to the steady-state kinetics analysis, the improved digestion of β-Lg was accompanied with the obvious decrease of antigenicity during the hydrolysis with pressure increasing, reflected by the increase of k c , the decrease of K m, the increase of overall catalytic efficiency (k c/K m), and the increase of the binding volume. It was indicated that although DHPM can increase the antigenicity of β-Lg, the enhanced digestibility of β-Lg at elevated pressure contributed to a decrease of antigenicity during the hydrolysis.

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Acknowledgments

This study was supported financially by the National Natural Science Foundation of China (21366021).

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None.

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This article does not contain any studies with human or animal subjects.

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Authors and Affiliations

  1. State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, 330047, China

    Junzhen Zhong, Shunjing Luo, Chengmei Liu & Wei Liu

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  1. Junzhen Zhong
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  2. Shunjing Luo
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  3. Chengmei Liu
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  4. Wei Liu
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Correspondence to Shunjing Luo.

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Zhong, J., Luo, S., Liu, C. et al. Steady-state kinetics of tryptic hydrolysis of β-lactoglobulin after dynamic high-pressure microfluidization treatment in relation to antigenicity. Eur Food Res Technol 239, 525–531 (2014). https://doi.org/10.1007/s00217-014-2248-2

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  • DOI: https://doi.org/10.1007/s00217-014-2248-2

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