Table 1.

Ultrasonic monitoring of thee proteolytic of the milk protease and milk proteins described in the literature.

Protease	Reactions and Conditions	Reference
Chymosin	Ultrasonic renneting process of milk at 30 °C. Ultrasonic analysis of multistage structural rearrangement.	[113]
Chymosin	Ultrasonic renneting process of milk at 30 °C. Comparison of effect of pH, temperature and enzyme-induced gelation in milks.	[114]
Chymosin	Ultrasonic renneting process of milk at 30 °C. Effect of preheat treatment at ultra-high temperature.	[116]
Proteinase K	Hydrolysis of Gly-Leu-Gly-Gly-Ala (synthetic pentapeptides) in 30-mM Tris buffer, pH 8, at 37 °C. Effect of substrate-enzyme ratio.	[109,119]
Proteinase K	Hydrolysis of bovine serum albumin (BSA) in 30-mM Tris buffer, pH 8, at 37 °C. Effect of enzyme concentration.	[109,119]
Proteinase K	Hydrolysis of bovine casein aggregates in 30-mM Tris buffer, pH 8, at 37 °C. Effect of substate concentration.	[109,119]
Chymosin (Maxiren® 180)	Proteolytic activity in milk samples at 30 °C. Screening method of enzyme activity.	[117]
Protease (Bakezyme B500®) a	Proteolytic activity in wheat flour suspension at 30 °C. Screening method of enzyme activity.	[117]
Trypsin	Hydrolysis of β-casein in 50-mM phosphate, pH 7.5, at 37 °C	[111]
Pancreatin	Proteolysis of casein solution at 37 °C. Effect of hydrolytic conditions relevant to pharmacopoeia assays.	[118]
α-chymotrypsin	Hydrolysis of β-lactoglobulin in 0.1-mol kg−1 phosphate buffer, pH 7.8, at 25 °C. Effect of substrate concentration.	[73]
Trypsin	Hydrolysis of β-casein in 0.1-mol kg−1 phosphate buffer. Effect of pH (6.6–8), temperature (15–45 °C) and trypsin concentration.	[104]

^a Neutral bacterial protease extract from Bacillus subtilis.