Enhancement of secreted production of glucoamylase through fed-batch bioreactor culture of recombinant yeast harboring glucose-controllable SUC2 promoter

Hyung Joon Cha; Kyoung Ro Kim; Byeong Hee Hwang; Dae Hee Ahn; Young Je Yoo

Korean Journal of Chemical Engineering, Vol.24, No.5, 812-815, September, 2007

DOI10.1007/s11814-007-0046-2 Export Citation

Enhancement of secreted production of glucoamylase through fed-batch bioreactor culture of recombinant yeast harboring glucose-controllable SUC2 promoter

Hyung Joon Cha^†, Kyoung Ro Kim, Byeong Hee Hwang, Dae Hee Ahn¹, and Young Je Yoo²

Department of Chemical Engineering, Pohang University of Sicence and Technology, Pohang 790-784, Korea
¹Department of Environmental Engineering and Biotechnology, Myongji University, Yongin 449-728, Korea
²School of Chemical and Biological Engineering, Seoul National University, Seoul 151-744, Korea

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Glucoamylase that hydrolyses starch to glucose is one of the important industrial enzymes for ethanol production industry. Therefore, genetic production of recombinant glucoamylase has been widely studied. Previously, we reported secreted production of Saccharomyces diastaticus-originated glucoamylase in Saccharomyces cerevisiase expression system using its own signal sequence and the SUC2 promoter that is regulated by glucose level in culture medium. In the present work, we performed a comparative study between batch and fed-batch bioreactor cultures for secreted production of recombinant glucoamylase. Through maintaining low glucose levels in the culture broth, we obtained about 7-fold higher secreted production levels of glucoamlyase in fed-batch culture. Fed-batch culture strategy also enhanced (~3.1-fold) secretion efficiency of recombinant glucoamylase in S. cerevisiae.

Keywords:Recombinant Yeast;Glucoamylase;SUC2 Promoter;Secreted Production;Fed-batch Culture

[References]

Kingsman SM, Kingsman AJ, Mellor J, Trends Biotechnol., 5, 53 (1987)
Hopkins RH, Waller Stein Lab. Comm., 21, 309 (1958)
Cha HJ, Yoo YJ, Korean J. Chem. Eng., 12(5), 567 (1995)
Cha HJ, Yoo YJ, Process Biochem., 31, 499 (1996)
Cha HJ, Choi SS, Yoo YJ, Bentley WE, Process Biochem., 32(8), 679 (1997)
Cha HJ, Kim MH, Kim SH, Yeo JS, Chae HJ, Yoo YJ, Process Biochem., 33(3), 257 (1998)
Yamashita I, Suzuki K, Fukui S, J. Bacteriol., 161, 567 (1985)
Chu FK, Maley F, J. Biol. Chem., 255, 6392 (1980)
Carlson M, Botstein D, Cell, 28, 145 (1982)
Patkar AY, Seo JH, Lim HC, Biotechnol. Bioeng., 41, 1066 (1993)
Cha HJ, Yoo YJ, Ahn JH, Kang HS, Biotechnol. Lett., 14, 747 (1992)
Vanoni M, Pokko D, Martegani E, Alberghina L, Biochem. Biophys. Res. Commun., 164, 1331 (1989)
Ahn JS, Kang DW, Hwang IK, Park SH, Mheen TI, Korean J. Microbiol., 30, 403 (1992)
Zsebo KM, Lu HS, Fieschko JC, Goldstein L, Davis J, Duker K, Syggs SV, Lai PH, Bitter GA, J. BIOL. CHEM., 261, 5858 (1986)

[Referenced By]

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[1] Kingsman SM, Kingsman AJ, Mellor J, Trends Biotechnol., 5, 53 (1987)

[2] Hopkins RH, Waller Stein Lab. Comm., 21, 309 (1958)

[3] Cha HJ, Yoo YJ, Korean J. Chem. Eng., 12(5), 567 (1995)

[4] Cha HJ, Yoo YJ, Process Biochem., 31, 499 (1996)

[5] Cha HJ, Choi SS, Yoo YJ, Bentley WE, Process Biochem., 32(8), 679 (1997)

[6] Cha HJ, Kim MH, Kim SH, Yeo JS, Chae HJ, Yoo YJ, Process Biochem., 33(3), 257 (1998)

[7] Yamashita I, Suzuki K, Fukui S, J. Bacteriol., 161, 567 (1985)

[8] Chu FK, Maley F, J. Biol. Chem., 255, 6392 (1980)

[9] Carlson M, Botstein D, Cell, 28, 145 (1982)

[10] Patkar AY, Seo JH, Lim HC, Biotechnol. Bioeng., 41, 1066 (1993)

[11] Cha HJ, Yoo YJ, Ahn JH, Kang HS, Biotechnol. Lett., 14, 747 (1992)

[12] Vanoni M, Pokko D, Martegani E, Alberghina L, Biochem. Biophys. Res. Commun., 164, 1331 (1989)

[13] Ahn JS, Kang DW, Hwang IK, Park SH, Mheen TI, Korean J. Microbiol., 30, 403 (1992)

[14] Zsebo KM, Lu HS, Fieschko JC, Goldstein L, Davis J, Duker K, Syggs SV, Lai PH, Bitter GA, J. BIOL. CHEM., 261, 5858 (1986)