Solubility of undigested proteins and their hydrolysates was investigated over a wide range of pH values from pH 2.0 to pH 10.0 as described by Tsumura et al. (2005) .
The emulsifying activity index (EAI) and emulsifying stability index (ESI) of the intact proteins, MPHs and PIHs are carried out according to the method of Pearce & Kinsella (1978) .
The microscopic observation of each emulsion (20 µl) was carried out after 24 h using a CX31-12C04 microscope (Motic 2048×1536 pixels, Olympus Co., Tokyo, Japan) . The emulsion images were captured by a charge-coupled device camera (Olympus Co., Tokyo, Japan) connected to the microscope.
Foam expansion (FE) and foam stability (FS) of undigested proteins and their hydrolysates were conducted referring to the method of Shahidi et al. (1995) .
Water binding capacity (WBC) was measured referring to Mac-Connel, Eastwood & Mitchell (1974) and the Oil binding capacity (OBC) was carried out according to Lin, Humbert & Sosulski (1974) .
The emulsifying activity index (EAI) and emulsifying stability index (ESI) of the intact proteins, MPHs and PIHs are carried out according to the method of Pearce & Kinsella (1978) .
The microscopic observation of each emulsion (20 µl) was carried out after 24 h using a CX31-12C04 microscope (Motic 2048×1536 pixels, Olympus Co., Tokyo, Japan) . The emulsion images were captured by a charge-coupled device camera (Olympus Co., Tokyo, Japan) connected to the microscope.
Foam expansion (FE) and foam stability (FS) of undigested proteins and their hydrolysates were conducted referring to the method of Shahidi et al. (1995) .
Water binding capacity (WBC) was measured referring to Mac-Connel, Eastwood & Mitchell (1974) and the Oil binding capacity (OBC) was carried out according to Lin, Humbert & Sosulski (1974) .