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Maruyama J, Ohnuma H, Yoshikawa A, et al. Production and product quality assessment of human hepatitis B virus pre-S2 antigen in submerged and solid-state cultures of Aspergillus oryzae. J Biosci Bioeng. 2000;90(1):118-20
Maruyama, J., Ohnuma, H., Yoshikawa, A., Kadokura, H., Nakajima, H., & Kitamoto, K. (2000). Production and product quality assessment of human hepatitis B virus pre-S2 antigen in submerged and solid-state cultures of Aspergillus oryzae. Journal of bioscience and bioengineering, 90(1), 118-20.
Maruyama, J, et al. "Production and product quality assessment of human hepatitis B virus pre-S2 antigen in submerged and solid-state cultures of Aspergillus oryzae." Journal of bioscience and bioengineering vol. 90,1 (2000): 118-20.
Maruyama J, Ohnuma H, Yoshikawa A, Kadokura H, Nakajima H, Kitamoto K. Production and product quality assessment of human hepatitis B virus pre-S2 antigen in submerged and solid-state cultures of Aspergillus oryzae. J Biosci Bioeng. 2000;90(1):118-20. PMID: 16232829.
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J Biosci Bioeng. 2000;90(1):118-20.

Production and product quality assessment of human hepatitis B virus pre-S2 antigen in submerged and solid-state cultures of Aspergillus oryzae.

Journal of bioscience and bioengineering

J Maruyama, H Ohnuma, A Yoshikawa, H Kadokura, H Nakajima, K Kitamoto

Affiliations

  1. Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.

PMID: 16232829

Abstract

Pre-S2 is a diagnostically important antigen of human hepatitis B virus (HBV). In order to produce pre-S2 antigen in Aspergillus oryzae, the gene [pre-S2]3, which encodes a tandemly triplicated repeat of pre-S2 polypeptides was fused with the partial glaA gene encoding glucoamylase lacking the starch-binding domain. In submerged culture, A. oryzae transformants carrying glaA-[pre-S2]3 secreted a heterogeneously glycosylated form of the fusion protein that was partially degraded. Contrarily, utilization of a wheat brain solid-state culture system resulted in the secretion of a homogeneous glycosylated form of the whole fusion protein. This is the first report of a dissimilarity in glycosylated modification between submerged and solid-state culture conditions in heterologous protein production in A. oryzae.

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