Characteristics and functionality enhancement by glycosylation of bitter melon (Momordica charantia) seed protein.

Abstract

Seeds of ripe bitter melon (Momordica charantia) contain approximately 30% protein. However, this protein, which is less functional than soy protein, may have desirable functionalities as a food ingredient after modification. Bitter melon seed protein isolate (BMSPI) was prepared under optimal extraction conditions (defatted meal to 1.3 M NaCl was 1:10 w/v; pH 9.0) and its functional properties were investigated before and after modification by glycosylation. Glycosylation was conducted at varying relative humidities (50%/65%/80%) and temperatures (40 °C/50 °C/60 °C) using a response surface central composite design. Degree of glycosylation (DG) ranged from 39.3 to 52.5%, 61.7 to 70.9%, and 81.2 to 94.8% at 40 °C, 50 °C, and 60 °C, respectively (P values < 0.0001). Denaturation temperatures of all DGs ranged from 111.6 °C to 114.6 °C, while unmodified/native BMSPI had a value of 113.2 °C. Surface hydrophobicity decreased to approximately 60% when the DG was maximal (94.8%). Solubility decreased almost 90% when the DG was maximal in comparison to the native BMSPI (62.0%). Emulsifying activity increased from 0.35 to 0.80 when the DGs were ≥80%, while emulsion stability increased from 63 to 72 min when the DGs were greater than 70%. A similar trend was observed with foaming capacity and foaming stability of the glycosylated proteins. This glycosylated BMSPI with improved emulsifying and foaming properties could be used as an ingredient in food products where such properties are required.