Characteristics and properties of co-precipitated protein and film based on Bambara groundnut protein isolate and fish skin acid-soluble collagen

Co-precipitated protein (CPP) from Bambara groundnut protein isolate (BGPI) and fish skin acid-soluble collagen (ASC) at different BGPI/ASC ratios (100:0, 75:25, 50:50, 25:75 and 0:100 (v/v)) were prepared and characterized. CPP of BGPI/ASC at ratio of 75:25 had higher solubility at acidic and alkaline pHs, compared to other CPP samples. All CPPs had good emulsifying properties. Based on protein patterns, the combination of major bands from BGPI and ASC in the resulting CPP sample was observed. CPP with BGPI/ASC at ratio of 75:25 showed higher surface hydrophobicity than those of other CPP samples. When the films from CPPs were fabricated, similar tensile strength ( p > 0.05) was observed, regardless of BGPI/ASC ratios. Nevertheless, film from CPP with BGPI/ASC ratio of 25:75 had higher elongation at break along with lower water vapor permeability ( p < 0.05), compared to other CPP films. All CPP films had bright-yellowish color. Increasing ASC ratio augmented ( p < 0.05) light transmission of resulting CPP films. FTIR spectra revealed that all CPP films had the similar pattern and functional groups. Therefore, the co-precipitated BGPI and ASC at appropriate ratio could improve properties of resulting proteins, especially for film forming ability. • Protein isolate and collagen were co-precipitated at different ratios. • Co-precipitated protein (CPP) samples had good emulsifying and film properties. • All CPP films had bright-yellowish color and high UV light barrier properties. • Film from CPP at 25:75 showed higher elongation at break and water vapor barrier.