Biochemical characterization of highly organic solvent-tolerant cutinase from Fusarium oxysporum

被引:16
|
作者
Speranza, Paula [1 ]
Macedo, Gabriela Alves [1 ]
机构
[1] Univ Estadual Campinas, Fac Food Engn, Dept Food Sci, Rua Monteiro Lobato,80 Caixa Postal 6121, BR-13083970 Campinas, SP, Brazil
关键词
Enzyme; Cutinase; Fusarium oxysporum; Characterization; Organic solvent;
D O I
10.1016/Lbcab.2013.06.005
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Biochemical characterization of cuLinase from Fusuriurn oxysporum produced by submerged fermentation indicated that the enzyme showed a significant increase in activity, after exposure for 1 h in organic solvents, especially octanol, 2-nonanol, hexane, octane, isooctane and decane. After exposure to these solvents, the enzyme activity was higher by more than 40% when compared with the control without exposure to organic solvents. The highest activity observed in organic solvents, indicates the great potential of this enzyme in non-aqueous systems. The enzyme retained its activity almost completely in the temperature range between 28 and 50 degrees C, maintaining its activity more than 80% after 1 h at these temperatures. The enzyme retained its activity superior to 50% in the pH range between 5.6 and 7.0 after 24 h at 30 degrees C. The multivariate study showed that the activity is higher at temperature of 28 degrees C and pH 6.0. The enzyme has been activated in most metal ions tested, with the best result observed in the presence of Na+ (1 mM). The enzyme exhibited low activity in the ionic liquids tested (BMIM-PF4, BMIM-PF6). The presence of sodium oxalate, sodium citrate, sodium bisulfite and sodium azide (1 mM), significantly increased the activity of the enzyme, indicating that these salts bind to certain metal ions, which interfere with the action of the enzyme. The biochemical properties observed, indicating the potential of this enzyme for industrial and biotechnological applications. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:372 / 376
页数:5
相关论文
共 50 条
  • [31] Biochemical characterization of an organic solvent-tolerant glycosyltransferase from Bacillus licheniformis PI15 with potential application for raspberry ketone glycoside production
    Li, Bingfeng
    Fan, Bo
    Fan, Jingping
    Chang, Siyuan
    Pan, Xin
    Wang, Yinan
    Wu, Yaming
    Song, Junsong
    He, Xuejun
    BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY, 2020, 67 (02) : 249 - 256
  • [32] Refolding, purification and characterization of an organic solvent-tolerant lipase from Serratia marcescens ECU1010
    Li, Suxia
    Pang, Huaiyu
    Lin, Kang
    Xu, Jianhe
    Zhao, Jian
    Fan, Liqiang
    JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2011, 71 (3-4) : 171 - 176
  • [33] Production, Characterization, and Application of an Organic Solvent-Tolerant Lipase Present in Active Inclusion Bodies
    Suxia Li
    Kang Lin
    Huaiyu Pang
    Yixin Wu
    Jianhe Xu
    Applied Biochemistry and Biotechnology, 2013, 169 : 612 - 623
  • [34] Production, Characterization, and Application of an Organic Solvent-Tolerant Lipase Present in Active Inclusion Bodies
    Li, Suxia
    Lin, Kang
    Pang, Huaiyu
    Wu, Yixin
    Xu, Jianhe
    APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, 2013, 169 (02) : 612 - 623
  • [35] Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010
    Zhao, Li-Li
    Xu, Jian-He
    Zhao, Jian
    Pan, Jiang
    Wang, Zhi-Long
    PROCESS BIOCHEMISTRY, 2008, 43 (06) : 626 - 633
  • [36] Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Bacillus cereus BF-3
    Gang, Wang
    Guang, Chen
    Ming, Wu
    AFRICAN JOURNAL OF BIOTECHNOLOGY, 2011, 10 (61): : 13174 - 13179
  • [37] An Organic Solvent-Tolerant Alkaline Lipase from Cold-Adapted Pseudomonas mandelii: Cloning, Expression, and Characterization
    Kim, Junsung
    Jang, Sei-Heon
    Lee, Chang Woo
    BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 2013, 77 (02) : 320 - 323
  • [38] Microbial host selection and periplasmic folding in Escherichia coli affect the biochemical characteristics of a cutinase from Fusarium oxysporum
    Nikolaivits, Efstratios
    Kokkinou, Areti
    Karpusas, Michael
    Topakas, Evangelos
    PROTEIN EXPRESSION AND PURIFICATION, 2016, 127 : 1 - 7
  • [39] Purification and characterization of an organic solvent-tolerant and detergent-stable lipase from Haloferax mediterranei CNCMM 50101
    Akmoussi-Toumi, Siham
    Khemili-Talbi, Souad
    Ferioune, Imen
    Kebbouche-Gana, Salima
    INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2018, 116 : 817 - 830
  • [40] Characterization of an organic solvent-tolerant α-amylase from a halophilic isolate, Thalassobacillus sp. LY18
    Xin Li
    Hui-Ying Yu
    Folia Microbiologica, 2012, 57 : 447 - 453