Efficient Hydrolysis of Fish Parvalbumin by Marine Bacterial Protease VSP2V‐280: Allergen Removal

• Published in: Food science & nutrition 2025-01, Vol.13 (1), p.e4729-n/a
• Main Authors: Zhou, Junlan, Bai, Yue, Gao, Yuan, Tian, Huili, Wang, Ming'ao, Kang, Xinxin, Zhang, Lei, Lv, Mingsheng, Wang, Shujun
• Format: Article
• Language: English
• Subjects: allergen removal; Allergens; Allergies; Bacteria; Biotechnology industry; Calcium ions; cloning and expression; Cod; Detergents; E coli; enzymatic properties; Enzymes; Fish; Food; Heat; High temperature; Marine fish; Microorganisms; Original; Parvalbumin; Protease; Proteinase; Proteins
• ISSN: 2048-7177; 2048-7177
• DOI: 10.1002/fsn3.4729

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. Virgibacillus sp. SP2 produces protease that specifically removes parvalbumin. Protease gene VSP2V‐280 of Virgibacillus sp. SP2 was cloned and expressed in Escherichia. coli and screened for removal of parvalbumin. Ca2+ had a significant activating effect on VSP2V‐280 and it effectively promoted the removal of parvalbumin. VSP2V‐280 effectively removed parvalbumin from freshwater fish.