Physicochemical and emulsifying properties of mung bean protein isolate as influenced by succinylation

Figures & data

Table 1. Influence of succinic anhydride:protein ratio on the degree of N-acylation, ζ-potential, and surface hydrophobicity (S₀) of mung bean protein isolate (MPI). Means within a row with different superscripts are significantly different at p < 0.05.

	Succinic anhydride:MPI protein weight ratio
	0.00	0.01	0.03	0.05	0.07	0.10
N-Acylation (%)	0.00 ± 0.00a	8.78 ± 1.14b	15.03 ± 1.32c	24.19 ± 2.20d	30.32 ± 2.06e	39.87 ± 1.22f
ζ-Potential (mV)	−19.20 ± 0.70a	−20.57 ± 0.90a	−25.43 ± 0.70b	−28.57 ± 0.91c	−31.57 ± 0.80d	−32.62 ± 0.86d
Surface Hydrophobicity X 10^4	37.26 ± 0.35a	36.57 ± 0.35a	35.69 ± 0.44b	34.04 ± 0.29c	32.61 ± 1.01d	29.85 ± 0.36e

Figure 1. Influence of succinylation on the average particle size (Z-average) of mung bean protein isolate (MPI) at various succinic anhydride:protein ratios.

Figure 2. Influence of succinylation at the succinic anhydride:protein weight ratios of 0 (lane 1), 0.01 (lane 2), 0.03 (lane 3), 0.05 (lane 4), 0.07 (lane 5) and 0.10 (lane 6) on the SDS-PAGE patterns of MPI. Lane M is a protein marker.

Figure 3. Influence of succinylation on the exposed and total free sulfhydryl groups of mung bean protein isolate (MPI) at various succinic anhydride:protein ratios.

Figure 4. Influence of succinylation on solubility profiles of mung bean protein isolate (MPI) at various succinic anhydride:protein ratios.

Figure 5. Influence of succinylation on the emulsifying activity index (EAI) and emulsion stability index (ESI) of mung bean protein isolate (MPI) at various succinic anhydride:protein ratios.