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

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Author list: Nilantha Lakshman P.L., Tachibana S., Toyama H., Taira T., Suganuma T., Suntornsuk W., Yasuda M.

Publisher: Oxford University Press

Publication year: 2011

Journal: Journal of Industrial Microbiology and Biotechnology (1367-5435)

Volume number: 38

Issue number: 9

Start page: 1485

End page: 1492

Number of pages: 8

ISSN: 1367-5435

eISSN: 1476-5535

URL: https://www.scopus.com/inward/record.uri?eid=2-s2.0-80052457641&doi=10.1007%2fs10295-010-0933-0&partnerID=40&md5=5987696792d9c9756e08b733a77d26b6

Languages: English-Great Britain (EN-GB)

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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, Gln 4-His 5, His 10-Leu 11, Ala 14-Leu 15, Gly 23-Phe 24 and Phe 24-Phe 25 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. © 2011 Society for Industrial Microbiology.

Keywords

Acid proteinase, Antigenicity, Monascus purpureus, Preservation stability, Tofuyo, Whey protein