Analysis of Gene Expression in Yeast Protoplasts Using DNA Microarrays and Their Application for Efficient Production of Invertase and α-Glucosidase (BIOCHEMICAL ENGINEERING)

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概要

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• The global gene expression of cultured Saccharomyces cerevisiae protoplasts was compared with that of cells using DNA microarray. Quantitative and qualitative analyses revealed that after 6h of cultivation, 416 gene transcript levels (about 7.1% in all) in the cultured protoplasts were different from those in the cells. Various characteristics and functions of the protoplasts were predicted from the analysis of the gene functions. The cultured protoplasts were more sensitive to oxidative stress than the cultured cells. Their cell cycles were arrested at the G1 phase and cell wall synthesis was promoted. Carbohydrate metabolism was activated in cultured protoplasts, while amino acid biosynthesis was inhibited. Furthermore, some genes associated with the secretory pathway of metabolites were activated, leading to active secretion of these metabolites into the broth. As an example of the application of DNA microarray analysis, we developed two novel methods for the production of useful enzymes based on the characteristics of protoplasts. One was the production of in vertase based on the activated secretory pathway, while the other was the production of α-glucosidase based on the activated carbohydrate metabolism. The secretion of invertase and α-glucosidase was promoted in cultured protoplasts. The invertase and α-glucosidase productivities in the cultured protoplasts were 657 U and 218 U, respectively. On the other hand, only 227 U of invertase was produced, while α-glucosidase was not detected, in the cultured cells. The fragile protoplasts were immobilized in agarose gel to protect them from hydrodynamic stress. Four repeated-batch cultures with the immobilized protoplasts were performed, leading to the production of 1574 U of invertase and 739 U of α-glucosidase. The same productivities were obtained when this system was scaled up by 10-fold (invertase : 13304 U ; α-glucosidase : 7688 U).

• 社団法人日本生物工学会の論文
• 2004-03-25

著者

• Aoyagi H

  Institute Of Applied Biochemistry University Of Tsukuba

• Aoyagi Hideki

  Institute Of Life Science And Bioengineering Graduate School Of Life And Environmental Science Unive

• Aoyagi Hideki

  Institute Of Applied Biochemistry University Of Tsukuba

• Aoyagi H

  Univ. Tsukuba Ibaraki Jpn

• Tanaka Hideo

  Institute Of Life Science And Bioengineering Graduate School Of Life And Environmental Science Unive

• Iwasaki K

  National Institute For Environmental Studies

• MERA NOBUAKI

  Institute of Applied Biochemistry, University of Tsukuba

• NAKASONO SATOSHI

  Bio-Science Department, Central Research Institute of Electric Power Industry

• IWASAKI KAZUHIRO

  National Institute for Environmental Studies

• SAIKI HIROSHI

  Bio-Science Department, Central Research Institute of Electric Power Industry

• Mera Nobuaki

  Institute Of Applied Biochemistry University Of Tsukuba

• Nakasono Satoshi

  Bio-science Department Central Research Institute Of Electric Power Industry

• Saiki Hiroshi

  Bio-science Department Central Research Institute Of Electric Power Industry

• Tanaka Hideo

  Institute For Biological Resources And Functions National Institute Of Advanced Industrial Science A

• Tanaka Hideo

  Institute Of Applied Biochemistry University Of Tsukuba

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