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      KCI등재 SCIE SCOPUS

      Whole Cell Biotransformation of 1-dodecanol by Escherichia coli by Soluble Expression of ADH Enzyme from Yarrowia lipolytica

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      https://www.riss.kr/link?id=A107396150

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      다국어 초록 (Multilingual Abstract)

      In this study, alcohol dehydrogenases (ADH) enzymes from Yarrowia lipolytica were investigated for the cloning, soluble expression, and biotransformation of 1-dodecanol to 1-dodecanal, which reaction was thermodynamically unfavorable. Sole expression of ADHs in Escherichia coli did not produce soluble form of cytosolic protein, in spite of the effort to solubilize ADH protein by optimizing IPTG concentration, temperature, and auto-induction medium. Eventually, the active form of soluble ADH proteins was successfully obtained through the co-expression of ADH with chaperone protein in pG-KJE8 vector. After analyzing the individual sets of optimization, it was determined that pET-28a(+)::adh coexpression with the pG-KJE8 molecular chaperone in LB medium with 0.1 mM IPTG, 4 mg/mL arabinose, and 2 ng/mL tetracycline achieved optimum expressions against all of the five ADH proteins. Finally, the whole cell biotransformation activity of ADH2 was determined in 1-dodecanol oxidation to 1-dodecanal, followed by further oxidation to 1-dodecanoic acid.
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      In this study, alcohol dehydrogenases (ADH) enzymes from Yarrowia lipolytica were investigated for the cloning, soluble expression, and biotransformation of 1-dodecanol to 1-dodecanal, which reaction was thermodynamically unfavorable. Sole expression ...

      In this study, alcohol dehydrogenases (ADH) enzymes from Yarrowia lipolytica were investigated for the cloning, soluble expression, and biotransformation of 1-dodecanol to 1-dodecanal, which reaction was thermodynamically unfavorable. Sole expression of ADHs in Escherichia coli did not produce soluble form of cytosolic protein, in spite of the effort to solubilize ADH protein by optimizing IPTG concentration, temperature, and auto-induction medium. Eventually, the active form of soluble ADH proteins was successfully obtained through the co-expression of ADH with chaperone protein in pG-KJE8 vector. After analyzing the individual sets of optimization, it was determined that pET-28a(+)::adh coexpression with the pG-KJE8 molecular chaperone in LB medium with 0.1 mM IPTG, 4 mg/mL arabinose, and 2 ng/mL tetracycline achieved optimum expressions against all of the five ADH proteins. Finally, the whole cell biotransformation activity of ADH2 was determined in 1-dodecanol oxidation to 1-dodecanal, followed by further oxidation to 1-dodecanoic acid.

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      참고문헌 (Reference)

      1 Park, H. A, "α, ω-Oxyfunctionalization of C12 alkanes via whole-cell biocatalysis of CYP153A from Marinobacter aquaeolei and a new CYP from Nocardia farcinica IFM10152" 156 : 107524-, 2020

      2 Liu, H. L, "The effect of metal ions on the binding of ethanol to human alcohol dehydrogenase beta2beta2" 10 : 302-312, 2003

      3 de Smidt, O, "The alcohol dehydrogenases of Saccharomyces cerevisiae: a comprehensive review" 8 : 967-978, 2008

      4 Kasprzak, K, "Synthesis of 1-(S)-phenylethanol and ethyl (R)-4-chloro-3-hydroxybutanoate using recombinant Rhodococcus erythropolis alcohol dehydrogenase produced by two yeast species" 106 : 107-117, 2016

      5 Nguyen, G. T, "Structural basis for broad substrate selectivity of alcohol dehydrogenase YjgB from Escherichia coli. Molecules" 25 : 2404-, 2020

      6 Pamidimarri D. V. N Sudheer, "Screening, Expression, and Characterization of Baeyer-Villiger Monooxygenases for the Production of 9-(nonanoyloxy)nonanoic Acid from Oleic Acid" 한국생물공학회 22 (22): 717-724, 2017

      7 Gutheil, W. G, "Purification, characterization, and partial sequence of the glutathionedependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase" 31 : 475-481, 1992

      8 Yoo, H. W, "Production of 12-hydroxy dodecanoic acid methyl ester using a signal peptide sequence-optimized transporter AlkL and a novel monooxygenase" 291 : 121812-, 2019

      9 Sudheer, P. D. V. N, "Production of (Z)-11-(heptanoyloxy)undec-9-enoic acid from ricinoleic acid by utilizing crude glycerol as sole carbon source in engineered Escherichia coli expressing BVMO-ADH-FadL" 119 : 45-51, 2018

      10 Wales, M. R, "NADP-dependent alcohol dehydrogenases in bacteria and yeast: purification and partial characterization of the enzymes from Acinetobacter calcoaceticus and Saccharomyces cerevisiae" 140 : 173-183, 1994

      1 Park, H. A, "α, ω-Oxyfunctionalization of C12 alkanes via whole-cell biocatalysis of CYP153A from Marinobacter aquaeolei and a new CYP from Nocardia farcinica IFM10152" 156 : 107524-, 2020

      2 Liu, H. L, "The effect of metal ions on the binding of ethanol to human alcohol dehydrogenase beta2beta2" 10 : 302-312, 2003

      3 de Smidt, O, "The alcohol dehydrogenases of Saccharomyces cerevisiae: a comprehensive review" 8 : 967-978, 2008

      4 Kasprzak, K, "Synthesis of 1-(S)-phenylethanol and ethyl (R)-4-chloro-3-hydroxybutanoate using recombinant Rhodococcus erythropolis alcohol dehydrogenase produced by two yeast species" 106 : 107-117, 2016

      5 Nguyen, G. T, "Structural basis for broad substrate selectivity of alcohol dehydrogenase YjgB from Escherichia coli. Molecules" 25 : 2404-, 2020

      6 Pamidimarri D. V. N Sudheer, "Screening, Expression, and Characterization of Baeyer-Villiger Monooxygenases for the Production of 9-(nonanoyloxy)nonanoic Acid from Oleic Acid" 한국생물공학회 22 (22): 717-724, 2017

      7 Gutheil, W. G, "Purification, characterization, and partial sequence of the glutathionedependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase" 31 : 475-481, 1992

      8 Yoo, H. W, "Production of 12-hydroxy dodecanoic acid methyl ester using a signal peptide sequence-optimized transporter AlkL and a novel monooxygenase" 291 : 121812-, 2019

      9 Sudheer, P. D. V. N, "Production of (Z)-11-(heptanoyloxy)undec-9-enoic acid from ricinoleic acid by utilizing crude glycerol as sole carbon source in engineered Escherichia coli expressing BVMO-ADH-FadL" 119 : 45-51, 2018

      10 Wales, M. R, "NADP-dependent alcohol dehydrogenases in bacteria and yeast: purification and partial characterization of the enzymes from Acinetobacter calcoaceticus and Saccharomyces cerevisiae" 140 : 173-183, 1994

      11 Dahlin, J, "Multi-omics analysis of fatty alcohol production in engineered yeasts Saccharomyces cerevisiae and Yarrowia lipolytica" 10 : 747-, 2019

      12 Koesoema, A. A, "Impact and relevance of alcohol dehydrogenase enantioselectivities on biotechnological applications" 104 : 2897-2909, 2020

      13 Kusano, M, "Hemiacetal dehydrogenation activity of alcohol dehydrogenases in Saccharomyces cerevisiae" 62 : 1956-1961, 1998

      14 Iwama, R, "Functional roles and substrate specificities of twelve cytochromes P450 belonging to CYP52 family in nalkane assimilating yeast Yarrowia lipolytica" 91 : 43-54, 2016

      15 Johnson, J, "Expression, purification and characterization of halophilic protease Pph_Pro1 cloned from Pseudoalteromonas phenolica" 152 : 46-55, 2018

      16 Danielsson, O, "Enzymogenesis”:classical liver alcohol dehydrogenase origin from the glutathionedependent formaldehyde dehydrogenase line" 89 : 9247-9251, 1992

      17 Han, C, "Enhanced matingtype switching and sexual hybridization in heterothallic yeast Yarrowia lipolytica" 20 : 2020

      18 Park, H, "Engineering of melanin biopolymer by co-expression of MelC tyrosinase with CYP102G4 monooxygenase: Structural composition understanding by 15 tesla FT-ICR MS analysis" 157 : 107530-, 2020

      19 Xu, P, "Engineering Yarrowia lipolytica as a platform for synthesis of drop-in transportation fuels and oleochemicals" 113 : 10848-10853, 2016

      20 Chang, Y. K, "Direct recovery of alcohol dehydrogenase from unclarified yeast cell homogenate by IDEBAC using an improved scheme for elution" 30 : 1-10, 2006

      21 Lee, H, "Development of a promising microbial platform for the production of dicarboxylic acids from biorenewable resources" 11 : 310-, 2018

      22 Choi, K. Y, "Consolidated conversion of protein waste into biofuels and ammonia using Bacillus subtilis" 23 : 53-61, 2014

      23 Ciriacy, M, "Cis-dominant regulatory mutations affecting the formation of glucose-repressible alcohol dehydrogenase (ADHII) in Saccharomyces cerevisiae" 145 : 327-333, 1976

      24 Lee, H., "Characterization of the newly isolated omega-oxidizing yeast Candida sorbophila DS02 and its potential applications in longchain dicarboxylic acid production" 101 : 6333-6342, 2017

      25 De Bolle, X, "Bivalent cations stabilize yeast alcohol dehydrogenase I" 323 : 409-413, 1997

      26 Ahsan, M. M, "Biosynthesis of the Nylon 12 monomer, omega-aminododecanoic acid with novel CYP153A, AlkJ, and omega-TA enzymes" 13 : e1700562-, 2018

      27 Lee, J. S, "Bioethanol production by heterologous expression of Pdc and AdhII in Streptomyces lividans" 97 : 6089-6097, 2013

      28 Iwama, R, "Alcohol dehydrogenases and an alcohol oxidase involved in the assimilation of exogenous fatty alcohols in Yarrowia lipolytica" 15 : 2015

      29 Jones, I. G, "ADHII in Aspergillus nidulans is induced by carbon starvation stress" 32 : 33-43, 2001

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      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2023 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2020-01-01 평가 등재학술지 유지 (해외등재 학술지 평가) KCI등재
      2011-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2009-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2007-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2004-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      2003-01-01 평가 등재후보 1차 PASS (등재후보1차) KCI등재후보
      2001-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      학술지 인용정보

      학술지 인용정보
      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 1.14 0.13 0.75
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.57 0.46 0.239 0.02
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