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Updated: Jun 2, 2025

Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens
Published on: February 24, 2021
Efficient Hydrolysis of Fish Parvalbumin by Marine Bacterial Protease VSP2V-280: Allergen Removal
Junlan Zhou1,2, Yue Bai1,2, Yuan Gao1,2
1Jiangsu Key Laboratory of Marine Bioresources and Environment/Jiangsu Key Laboratory of Marine Biotechnology Jiangsu Ocean University Lianyungang China.
Abstract:
Parvalbumin is a major allergen in fish. However, there is currently no effective and safe way to remove this allergen from fish. In this study, protease gene VSP2V-280 of marine bacteria Virgibacillus sp. SP2 was cloned and expressed. The protease enzyme showed maximum activity at 50°C and pH 10.0. Ca2+ and Cu2+ promoted the enzyme. The enzyme showed good parvalbumin degradation efficiency in fish. Based on the gel analysis, when 0.3 mg/mL of parvalbumin was incubated with protease VSP2V-280 (30 U/mL) containing 1 mM Ca2+ for 3 h, the parvalbumin removal rate reached 97%. The enzyme was further used for parvalbumin removal from Ctenopharyngodon idella, Pelteobagrus fulvidraco, Parabramis pekinensis, and Carassius auratus. The parvalbumin removal rate reached 93% in 4 h at an enzyme dosage of 72 U/mL. The study showed the potential of VSP2V-280 to remove parvalbumin from aquatic products.

