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Original Articles

Emulsifying Properties of Cross-Linking Between Proteins Extracted from Cold/Hot Pressed Peanut Meal and Hydrolysed Fish (Decapterus Maruadsi) Proteins

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Pages 1750-1762 | Received 27 Apr 2012, Accepted 23 Aug 2012, Published online: 24 Apr 2014

Figures & data

Figure 1  SDS-PAGE profile of samples without (lanes 1, 2, 5, 6) and with (lanes 3, 4, 7, 8) TGase treatment. Lane M: Molecular markers; Lane 1: CPPP; Lane 2: mMixture of CPPP and DPH; Lane 3: cCross-linked CPPP; Lane 4: cCross-linked CPPP and DPH; Lane 5: HPPP; Lane 6: mMixture of HPPP and DPH; Lane 7: cCross-linked HPPP; Lane 8: cCross-linked HPPP and DPH (CPPP: cold-pressed peanut protein; HPPP: hot-pressed peanut protein; DPH: Decapterus maruadsi hydrolysates).

Figure 1  SDS-PAGE profile of samples without (lanes 1, 2, 5, 6) and with (lanes 3, 4, 7, 8) TGase treatment. Lane M: Molecular markers; Lane 1: CPPP; Lane 2: mMixture of CPPP and DPH; Lane 3: cCross-linked CPPP; Lane 4: cCross-linked CPPP and DPH; Lane 5: HPPP; Lane 6: mMixture of HPPP and DPH; Lane 7: cCross-linked HPPP; Lane 8: cCross-linked HPPP and DPH (CPPP: cold-pressed peanut protein; HPPP: hot-pressed peanut protein; DPH: Decapterus maruadsi hydrolysates).

Table 1  The amino acid composition of CPPP, HPPP, and DPH

Figure 2  Particle size distribution of the emulsions made with (a) CPPP samples and (b) HPPP samples.

Figure 2  Particle size distribution of the emulsions made with (a) CPPP samples and (b) HPPP samples.

Figure 3  Effect of TGase treatment on the mean particle size d32 of emulsions. The columns having the same letter are insignificantly different (p > 0.05).

Figure 3  Effect of TGase treatment on the mean particle size d32 of emulsions. The columns having the same letter are insignificantly different (p > 0.05).

Figure 4  Microscopic structure of emulsions made with samples without (a, c, e, g) or with TGase (b, d, f, h) treatment observed by optical microscope at a magnification of 400×: (a) and (b), are cold-pressed peanut protein; (c) and (d), are hot-pressed peanut protein; (e) and (f), are cold-pressed peanut protein and Decapterus maruadsi hydrolysates; (g) and (h), are hot-pressed peanut protein and Decapterus maruadsi hydrolysates.

Figure 4  Microscopic structure of emulsions made with samples without (a, c, e, g) or with TGase (b, d, f, h) treatment observed by optical microscope at a magnification of 400×: (a) and (b), are cold-pressed peanut protein; (c) and (d), are hot-pressed peanut protein; (e) and (f), are cold-pressed peanut protein and Decapterus maruadsi hydrolysates; (g) and (h), are hot-pressed peanut protein and Decapterus maruadsi hydrolysates.

Figure 5  The changes in the mean particle size d43 of emulsions made with samples stored at room temperature for 20 days. The columns having the same letter are insignificantly different (p > 0.05).

Figure 5  The changes in the mean particle size d43 of emulsions made with samples stored at room temperature for 20 days. The columns having the same letter are insignificantly different (p > 0.05).

Figure 6  The changes in the creaming rate of emulsions made with samples stored at room temperature for 20 days. The columns having the same letter are insignificantly different (p > 0.05).

Figure 6  The changes in the creaming rate of emulsions made with samples stored at room temperature for 20 days. The columns having the same letter are insignificantly different (p > 0.05).

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