Hemoglobin(HB)is a valuable additive for enhancing the taste,flavor,and nutrition of plant-based protein products.With rising demand for sustainable and health-conscious food options,the exploration of novel HB source...Hemoglobin(HB)is a valuable additive for enhancing the taste,flavor,and nutrition of plant-based protein products.With rising demand for sustainable and health-conscious food options,the exploration of novel HB sources has become increasingly important to meet consumer needs.In this study,a plant-derived HB from Vigna angularis(VaHB)was heterologously expressed and characterized in Pichia pastoris.The data indicated that VaHB exhibited prominent absorption peaks at 415 and 540 nm,a secondary structure comparable to reference standards,high peroxidase activity(123.6 U/mg),and remarkable thermal stability(Tm=79.6℃).These attributes were found to differ from those of Glycine a HB(GmHB),an approved color additive in plant-based protein products.To optimize its production,the copy number of the globin-coding gene was enhanced and the entire heme biosynthesis pathway was reengineered,achieving a titer of 117.7 mg/L.These findings indicate that VaHB could be considered a comparable alternative to GmHB.展开更多
基金supported by the National Key Research and Devel-opment Program of China(2022YFD2101304)the Food Safety Risk Assessment Project from the National Health Commission of the PRC Specialty Laboratory of Food Safety Risk Assessment and Standard Development(RA-2024-2,RA-2025-2.1)+1 种基金the Start-up fund of Shanghai Jiao Tong University(WH220415004)the Shanghai Collaborative Innovation Center of Agri-Seeds(ZXWH3150101/002).
文摘Hemoglobin(HB)is a valuable additive for enhancing the taste,flavor,and nutrition of plant-based protein products.With rising demand for sustainable and health-conscious food options,the exploration of novel HB sources has become increasingly important to meet consumer needs.In this study,a plant-derived HB from Vigna angularis(VaHB)was heterologously expressed and characterized in Pichia pastoris.The data indicated that VaHB exhibited prominent absorption peaks at 415 and 540 nm,a secondary structure comparable to reference standards,high peroxidase activity(123.6 U/mg),and remarkable thermal stability(Tm=79.6℃).These attributes were found to differ from those of Glycine a HB(GmHB),an approved color additive in plant-based protein products.To optimize its production,the copy number of the globin-coding gene was enhanced and the entire heme biosynthesis pathway was reengineered,achieving a titer of 117.7 mg/L.These findings indicate that VaHB could be considered a comparable alternative to GmHB.
