Sword bean variants and different pretreatments influence protein extraction and protein properties

Figures & data

Table 1. Comparison of extract weights, protein concentrations and quantities between beans prepared with different pretreatments.

	Suspension (g/g bean)	Extract (g/g bean)	Residue (g/g bean)	Collection rate^a (%)	Protein concentration (mg/mL)	Protein quantity^b (mg protein/g dried bean)
WSBs
Untreated	9.0 ± 0.3^a	5.6 ± 0.1^b,c	1.8 ± 0.3^a	82.2	16.6 ± 1.2^a	93.0 ± 6.7^a,b
Drilled	9.6 ± 0.6^a	7.2 ± 0.4^a	1.5 ± 0.2^a,b	90.6	13.1 ± 1.1^b,c	94.0 ± 7.9^a
Milled	7.5 ± 1.0^b	5.1 ± 0.8^c	1.1 ± 0.1^b	82.7	14.5 ± 0.6^a,b	74.1 ± 3.1^c
RSBs
Untreated	−	−	−	−	−	−
Drilled	9.5 ± 0.1^a	6.6 ± 0.3^a,b	1.6 ± 0.2^a,b	86.3	11.7 ± 0.9^c	77.3 ± 5.9^b,c
Milled	7.5 ± 0.3^b	4.9 ± 0.1^c	1.2 ± 0.1^b	81.3	13.2 ± 1.2^b,c	52.7 ± 4.8^d

^aThe collection rate was estimated by dividing the total extract and waste weight by the weight of the suspension.

^bProtein quantities in the extract were determined by multiplying the protein concentration by the extract volume.

Values are expressed as means ± SD for three different experiments. Means within the same column bearing different superscripted roman letters are significantly different, with p < 0.05 determined by analysis of variance using the Tukey–Kramer test.

Figure 1. Comparison of canavalin solubility changes.

The canavalin solubility in the extracts was analyzed by SDS-PAGE after addition of MgCl₂ to WSB and RSB extracts. The proportion of residual canavalin in the supernatant was estimated from the band intensity using Image J software. The data for WSBs (A) and RSBs (B) were plotted. The open circles indicate data for untreated WSBs that were only treated by soaking. The open triangles indicate drilled WSBs. The open squares represent milled WSBs. The closed triangles indicate drilled RSBs. The closed squares represent milled RSBs. Data are expressed as the average ± standard deviation of three independent experiments.