Abstract
The hydrolysis of milk proteins by the recombinant AprX‐SK37 protease and the changes in the rheological properties of the milk gel generated with AprX‐SK37 and glucono‐δ‐lactone (GDL) were investigated. The AprX‐SK37 and rennet selectively hydrolysed κ‐casein to yield a 16‐kDa band, while subtilisin hydrolysed all of the casein components. Milk treated only with AprX‐SK37 formed softer gel. Storage modulus (G′) values of the combined gels increased with GDL concentrations up to 7 g/L. High tan δ was observed in the combined gel at 8.75 g/L GDL alongside syneresis. AprX‐SK37 is a promising milk‐clotting enzyme when combined with an optimal GDL concentration.
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