TY - JOUR
T1 - Chitosanase displayed on liposome can increase its activity and stability.
AU - Ngo, Kien Xuan
AU - Umakoshi, Hiroshi
AU - Shimanouchi, Toshinori
AU - Sugaya, Hiroyuki
AU - Kuboi, Ryoichi
N1 - Funding Information:
The fundamental concept of this study was supported by the Research Group of “Membrane Stress Biotechnology”. It was partially supported by a Grant-in-Aid for Scientific Research (Nos. 19656203, 19656220, 20360350, 20760539, 21246121) from the Ministry of Education, Culture, Sports, Science and Technology of Japan, a grant from the Global COE program Bio-Environment Chemistry of Japan Society for the Promotion of Science (JSPS). The authors are grateful to the Research Center for Solar Energy Chemistry of Osaka University and the Gas Hydrate Analyzing System of Osaka University. One of the authors (K.X. Ngo) also deeply acknowledges the financial support of JSPS.
PY - 2010/4/1
Y1 - 2010/4/1
N2 - The strategy to prepare a novel biocatalyst by the immobilization of chitosanase onto liposome (ICL) was carried out based on the direct interaction of liposomes with cell membrane of Streptomyces griseus cell. The ICL was characterized in relation to the molecular weight of protein, the chitosanase activity, the effect of the surface hydration of various liposomes on hydrolysis activity of immobilized chitosanase and the stability of ICL under various extreme conditions. The SDS-PAGE analysis of the purified ICL sample shows the existence of a protein with approximately 39kDa that corresponded to the sum of weight of the mature chitosanase and its signal peptide (38.8kDa). The above protein of ICL also expresses the chitosanase activity that is significantly higher than that of the conventional chitosanase. Furthermore, the surface hydration of liposomes used to prepare ICL that affected the activity of immobilized chitosanase verified the importance of liposome surfaces. Indeed, the stability of ICL assayed by measuring the chitosanase activity is significantly higher than that of conventional chitosanase under various temperatures and pH conditions. These characteristics of ICL show the possible preparation of the biocatalysts that can be prepared by immobilizing enzymes onto liposome vesicles properly.
AB - The strategy to prepare a novel biocatalyst by the immobilization of chitosanase onto liposome (ICL) was carried out based on the direct interaction of liposomes with cell membrane of Streptomyces griseus cell. The ICL was characterized in relation to the molecular weight of protein, the chitosanase activity, the effect of the surface hydration of various liposomes on hydrolysis activity of immobilized chitosanase and the stability of ICL under various extreme conditions. The SDS-PAGE analysis of the purified ICL sample shows the existence of a protein with approximately 39kDa that corresponded to the sum of weight of the mature chitosanase and its signal peptide (38.8kDa). The above protein of ICL also expresses the chitosanase activity that is significantly higher than that of the conventional chitosanase. Furthermore, the surface hydration of liposomes used to prepare ICL that affected the activity of immobilized chitosanase verified the importance of liposome surfaces. Indeed, the stability of ICL assayed by measuring the chitosanase activity is significantly higher than that of conventional chitosanase under various temperatures and pH conditions. These characteristics of ICL show the possible preparation of the biocatalysts that can be prepared by immobilizing enzymes onto liposome vesicles properly.
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U2 - 10.1016/j.jbiotec.2010.01.014
DO - 10.1016/j.jbiotec.2010.01.014
M3 - Article
C2 - 20100524
AN - SCOPUS:77953934891
VL - 146
SP - 105
EP - 113
JO - Journal of Biotechnology
JF - Journal of Biotechnology
SN - 0168-1656
IS - 3
ER -