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Figure 1. 

Peptide molecular weight distribution of various protein samples upon different hydrolysis time. (a) WPI; (b) SC; (c) EWP; (d) GE; (e) SPI; (f) PPI. * Molecular weights of native proteins were reported from literature^[49−54].

Figure 2. 

Standard splat assay microscopic image at 40× for PEG (negative control), and GE, SPI, SC, EWP and PPI hydrolysates after 15-min alcalase hydrolysis at 4% (w/w) concentration, and phosphate buffer saline (PBS – the buffer solvent) annealed at −8 °C for 30 min (scale bar = 50 μm).

Figure 3. 

Mean average ice crystal size (μm) from different protein hydrolysates (4% w/w) solutions under −8 °C. Same lower-case letter indicate no significant difference (p > 0.05) within the same hydrolysis time, while same upper-case letters indicate no significant difference within the same protein (p > 0.05).

Figure 4. 

Ice crystal size of 4% (a) SPI-15 and (b) SPI-60 hydrolysates in PBS buffer system annealed under −10 to −4 °C for various time. (c) Ice crystal size of 4% PEG (negative control) after 30 min annealing under various temperatures.

Figure 5. 

Ice crystal size of SPI-15 hydrolysates in PBS buffer at varied concentrations (2%−4% w/w) annealed under different temperatures (−10 to −4 °C) for 30 min.

Figure 6. 

Ice crystal image under polarized microscope at 40x for 4% SPI hydrolysates, PPI hydrolysates and their OSA-modified derivatives annealed at −8 °C compared to the negative control 4% PEG and PBS (the buffer solvent). (scale bar = 50 μm).

Figure 7. 

Ice crystal growth within 30 min annealed at −8 °C and −6 °C in 4% (w/w) (a) SPI-12hr hydrolysate and OSA modified SPI-12hr, and (b) PPI-12hr hydrolysate and OSA modified PPI-12hr.