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Stabilization of enzymes by the recombinant 30Kc19 protein

Cited 18 time in Web of Science Cited 18 time in Scopus
Authors
Park, Ju Hyun; Park, Hee Ho; Choi, Shin Sik; Park, Tai Hyun
Issue Date
2012-01
Publisher
Elsevier Ltd.
Citation
Process Biochemistry Vol.47 No.1, pp. 164-169
Keywords
복합학Enzyme stability30Kc19Bovine serum albuminAlkaline phosphataseHorseradish peroxidase
Abstract
In previous studies, we reported that the 3019 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. (C) 2011 Elsevier Ltd. All rights reserved.
ISSN
1359-5113
Language
English
URI
http://hdl.handle.net/10371/83143
DOI
https://doi.org/10.1016/j.procbio.2011.10.022
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College of Engineering/Engineering Practice School (공과대학/대학원)Dept. of Chemical and Biological Engineering (화학생물공학부)Journal Papers (저널논문_화학생물공학부)
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