Efficient co-displaying and artificial ratio control of α-amylase and glucoamylase on the yeast cell surface by using combinations of different anchoring domains
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| 024 | 7 | 0 | |a 10.1007/s00253-014-6250-1 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00253-014-6250-1 | ||
| 245 | 0 | 0 | |a Efficient co-displaying and artificial ratio control of α-amylase and glucoamylase on the yeast cell surface by using combinations of different anchoring domains |h [Elektronische Daten] |c [Kentaro Inokuma, Takanobu Yoshida, Jun Ishii, Tomohisa Hasunuma, Akihiko Kondo] |
| 520 | 3 | |a Recombinant yeast strains that display heterologous amylolytic enzymes on their cell surface via the glycosylphosphatidylinositol (GPI)-anchoring system are considered as promising biocatalysts for direct ethanol production from starchy materials. For the effective hydrolysis of these materials, the ratio optimization of multienzyme activity displayed on the cell surface is important. In this study, we have presented a ratio control system of multienzymes displayed on the yeast cell surface by using different GPI-anchoring domains. The novel gene cassettes for the cell-surface display of Streptococcus bovis α-amylase and Rhizopus oryzae glucoamylase were constructed using the Saccharomyces cerevisiae SED1 promoter and two different GPI-anchoring regions derived from Saccharomyces cerevisiae SED1 or SAG1. These gene cassettes were integrated into the Saccharomyces cerevisiae genome in different combinations. Then, the cell-surface α-amylase and glucoamylase activities and ethanol productivity of these recombinant strains were evaluated. The combinations of the gene cassettes of these enzymes affected the ratio of cell-surface α-amylase and glucoamylase activities and ethanol productivity of the recombinant strains. The highest ethanol productivity from raw starch was achieved by the strain harboring one α-amylase gene cassette carrying the SED1-anchoring region and two glucoamylase gene cassettes carrying the SED1-anchoring region (BY-AASS/GASS/GASS). This strain yielded 22.5 ± 0.6g/L of ethanol from 100g/L of raw starch in 120h of fermentation. | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2014 | ||
| 690 | 7 | |a Saccharomyces cerevisiae |2 nationallicence | |
| 690 | 7 | |a Cell-surface display |2 nationallicence | |
| 690 | 7 | |a α-Amylase |2 nationallicence | |
| 690 | 7 | |a Glucoamylase |2 nationallicence | |
| 690 | 7 | |a Ratio control |2 nationallicence | |
| 700 | 1 | |a Inokuma |D Kentaro |u Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan |4 aut | |
| 700 | 1 | |a Yoshida |D Takanobu |u Technology Research Association of Highly Efficient Gene Design, Integrated Research Center of Kobe University 108, 7-1-48 Minatojimaminamimachi, Chuo-ku, 650-0047, Kobe, Japan |4 aut | |
| 700 | 1 | |a Ishii |D Jun |u Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan |4 aut | |
| 700 | 1 | |a Hasunuma |D Tomohisa |u Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan |4 aut | |
| 700 | 1 | |a Kondo |D Akihiko |u Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan |4 aut | |
| 773 | 0 | |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/4(2015-02-01), 1655-1663 |x 0175-7598 |q 99:4<1655 |1 2015 |2 99 |o 253 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00253-014-6250-1 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00253-014-6250-1 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Inokuma |D Kentaro |u Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Yoshida |D Takanobu |u Technology Research Association of Highly Efficient Gene Design, Integrated Research Center of Kobe University 108, 7-1-48 Minatojimaminamimachi, Chuo-ku, 650-0047, Kobe, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Ishii |D Jun |u Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Hasunuma |D Tomohisa |u Organization of Advanced Science and Technology, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Kondo |D Akihiko |u Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, 1-1 Rokkodai, Nada, 657-8501, Kobe, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/4(2015-02-01), 1655-1663 |x 0175-7598 |q 99:4<1655 |1 2015 |2 99 |o 253 | ||