Stabilization of enzymes by the recombinant 30Kc19 protein

Ju Hyun Park, Hee Ho Park, Shin Sik Choi, Tai Hyun Park

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26 Scopus citations


In previous studies, we reported that the 30K protein originating from the silkworm inhibited apoptosis in mammalian cells. In this work, we demonstrated that the 30Kc19 protein, which is most abundant 30K protein in silkworm hemolymph, also enhanced enzyme stability. When the recombinant 30Kc19 protein was supplemented into distilled-deionized water containing alkaline phosphatase or horseradish peroxidase, deactivation of both enzymes induced by non-buffered DDW was significantly suppressed. The increase in enzyme stability due to the presence of 30Kc19 was similar to that observed for bovine serum albumin, which is commonly used in conventional enzyme reactions. The decrease in enzyme activity due to long-term storage in different buffer systems was also inhibited by 30Kc19. The 30Kc19 protein structure was shown to play a vital role in stabilizing the enzyme. These results imply that the recombinant 30Kc19 protein hold promise for use as an additive to increase or maintain enzyme activity.

Original languageEnglish
Pages (from-to)164-169
Number of pages6
JournalProcess Biochemistry
Issue number1
StatePublished - Jan 2012

Bibliographical note

Funding Information:
This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (MEST) (No. 2010K001137 , 2010-0000825 , 2010-0020821 ). This work was also supported by WCU (World Class University) program through the Korea Science and Engineering Foundation funded by the Ministry of Education, Science and Technology ( R32-2010-000-10213-0 ).


  • 30Kc19
  • Alkaline phosphatase
  • Bovine serum albumin
  • Enzyme stability
  • Horseradish peroxidase


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