Stabilization of enzymes by the recombinant 30Kc19 protein

作者：Park Ju Hyun; Park Hee Ho; Choi Shin Sik; Park Tai Hyun^*

来源：Process Biochemistry, 2012, 47(1): 164-169.

DOI：10.1016/j.procbio.2011.10.022

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

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.

• 出版日期2012-1