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Application of an acid proteinase from Monascus purpureus to reduce antigenicity of bovine milk whey protein

  • Original Paper
  • Published:
Journal of Industrial Microbiology & Biotechnology

Abstract

An acid proteinase from Monascus purpureus No. 3403, MpuAP, was previously purified and some characterized in our laboratory (Agric Biol Chem 48:1637–1639, 1984). However, further information about this enzyme is lacking. In this study, we investigated MpuAP’s comprehensive substrate specificity, storage stability, and prospects for reducing antigenicity of whey proteins for application in the food industry. MpuAP hydrolyzed primarily five peptide bonds, Gln4–His5, His10–Leu11, Ala14–Leu15, Gly23–Phe24 and Phe24–Phe25 in the oxidized insulin B-chain. The lyophilized form of the enzyme was well preserved at 30–40°C for 7 days without stabilizers. To investigate the possibility of reducing the antigenicity of the milk whey protein, enzymatic hydrolysates of the whey protein were evaluated by inhibition ELISA. Out of the three main components of whey protein, casein and α-lactalbumin were efficiently degraded by MpuAP. The sequential reaction of MpuAP and trypsin against the whey protein successfully degraded casein, α-lactalbumin and β-lactoglobulin with the highest degree of hydrolysis. As a result, the hydrolysates obtained by using the MpuAP–trypsin combination showed the lowest antigenicity compared with the single application of pepsin, trypsin or pepsin–trypsin combination. Therefore, the overall result suggested that the storage-stable MpuAP and trypsin combination will be a productive approach for making hypoallergic bovine milk whey protein hydrolysates.

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Acknowledgments

This work was supported by the program for development and functional analysis of health food materials with Koji from the Ministry of Education, Sports, Science and Technology of Japan. Part of this work was carried out in the Asian Core Program of Yamaguchi University and Khon Kaen University, granted by the Japan Society for the Promotion of Science (JSPS) and the National Research Council of Thailand (NRCT).

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Authors and Affiliations

  1. United Graduate School of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan

    P. L. Nilantha Lakshman

  2. Department of Bioscience and Biotechnology, Faculty of Agriculture, University of the Ryukyus, 1 Senbaru, Nishihara-cho, Okinawa, 903-0213, Japan

    Shinjiro Tachibana, Hirohide Toyama, Toki Taira & Masaaki Yasuda

  3. Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima, 890-0065, Japan

    Toshihiko Suganuma

  4. Department of Microbiology, Faculty of Science, King Monkut’s University of Technology Thonburi, Bangmod, Thungkru, Bangkok, 10140, Thailand

    Worapot Suntornsuk

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  1. P. L. Nilantha Lakshman
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  2. Shinjiro Tachibana
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  3. Hirohide Toyama
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  5. Toshihiko Suganuma
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  7. Masaaki Yasuda
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Correspondence to Masaaki Yasuda.

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Nilantha Lakshman, P.L., Tachibana, S., Toyama, H. et al. Application of an acid proteinase from Monascus purpureus to reduce antigenicity of bovine milk whey protein. J Ind Microbiol Biotechnol 38, 1485–1492 (2011). https://doi.org/10.1007/s10295-010-0933-0

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  • DOI: https://doi.org/10.1007/s10295-010-0933-0

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