Cited by 8Proteins in Food SystemsEnzyme Production and CharacterizationPolysaccharides Composition and Applications

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

Rangnoi, Kuntalee, Phrommao, Ekkarat, Yamabhai, Montarop, Yongsawatdigul, Jirawat·2014·International Journal of Dairy Technology

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.

Integrity signals

Registry

Crossref · 10.1111/1471-0307.12145

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30 of 30 references verified0 citation errors · 0 not checkable

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Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • The increased optimal temperature for milk-clotting activity compared with proteolytic activity was likely the result of synergistic effects of κ-casein destabilization by the enzyme and heat treatment.

    “The increased optimal temperature for milk-clotting activity compared with PA was likely the result of the synergistic effects of κ-CN destabilization by the enzyme and heat treatment (Rangnoi et al., 2014;Hang et al., 2016).”
  • The firmness of the gel produced by microbial coagulants is lower than that produced by calf rennet.

    “Previous studies (Jacob et al., 2011;Hayaloglu et al., 2014;Rangnoi et al., 2014;Zhang et al., 2019) have shown that the firmness of the gel produced by microbial coagulants is lower than that produced by calf rennet.”
  • Milk treated with recombinant AprX-SK37 protease from Virgibacillus spp. SK37 formed a softer gel than milk gel treated with rennet.

    “In a study by Rangnoi et al. (2014), milk treated with recombinant AprX-SK37 protease from Virgibacillus spp.SK37 formed a softer gel than milk gel treated with rennet.”

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Authors
Rangnoi, K., Phrommao, E., Yamabhai, M., & Yongsawatdigul, J.
Affiliations
Suranaree University of Technology (TH)
Corresponding author
Yongsawatdigul, Jirawat
Venue
International Journal of Dairy Technology
Publisher
Wiley
Published
2014-06-24
Volume
67
Issue
4
Pages
547-553
ISSN
  • 1364-727X (ISSN-L)
  • 1471-0307
OpenAlex
W2148337242
Cited by
8
References
30
Citations by year
2025: 1 · 2023: 5 · 2019: 1 · 2016: 1
FWCI
0.48
Type
journal article
Language
en
Open access
closed
Locations
International Journal of Dairy Technology (publishedVersion)
Funders
Higher Education Research Promotion and National Research University Project of Thailand, Office of the Higher Education Commission.
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
Keywords
milk gels, Virgibacillus, moderately halophilic bacteria, glucono-δ-lactone, κ-casein hydrolysis, milk-clotting enzyme, gel rheology, storage modulus, syneresis, rennet, subtilisin, recombinant protease

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