Abstract
Capillary electrophoresis using an untreated fused-silica capillary and a low-pH buffer containing urea and hydroxypropyl methyl cellulose was used to follow the proteolytic action of neutral protease of Bacillus subtilis on isolated casein fractions and whole milk casein (CN) samples. Electrophoretic analysis showed that this protease caused intense hydrolysis of α-CN, β-CN and κ-CN. The breakdown products due to the attack of the neutral protease on β-CN, γ 2-CN A, γ 1-CN B, γ 1-CN A 1, γ 3-CN B, γ 1-CN A 2, γ 3-CN A, β-CN-I A 1, β-CN-I A 2 and β-CN-I B, and on α s-CN, α s1-CN-I, α s0-CN-I and α s1-CN f(1–23) were separated.
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