Combined milk gel generated with a novel coagulating enzyme by  Virgibacillus  sp. SK37, a moderately halophilic bacterium | Zendy

Rangnoi Kuntalee | Zendy; Phrommao Ekkarat | Zendy; Yamabhai Montarop | Zendy; Yongsawatdigul Jirawat | Zendy

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Combined milk gel generated with a novel coagulating enzyme by Virgibacillus sp. SK37, a moderately halophilic bacterium

Author(s) -

Rangnoi Kuntalee,

Phrommao Ekkarat,

Yamabhai Montarop,

Yongsawatdigul Jirawat

Publication year - 2014

Publication title -

international journal of dairy technology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.061

H-Index - 53

eISSN - 1471-0307

pISSN - 1364-727X

DOI - 10.1111/1471-0307.12145

Subject(s) - syneresis , rennet , chemistry , casein , hydrolysis , food science , chromatography , protease , enzyme , biochemistry

The hydrolysis of milk proteins by the recombinant AprX‐SK37 protease and the changes in the rheological properties of the milk gel generated with A pr X ‐ SK 37 and glucono‐δ‐lactone ( GDL ) were investigated. The A pr X ‐ SK 37 and rennet selectively hydrolysed κ‐casein to yield a 16‐kDa band, while subtilisin hydrolysed all of the casein components. Milk treated only with A pr X ‐ SK 37 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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