Effect of Additives on Transesterification Activity of Rhizopus chinensis Lipase.

Yasuda, Masahiro; Kiguchi, Taro; Kasahara, Hiroki; Ogino, Hiroyasu; Ishikawa, Haruo

doi:10.1263/jbb.90.681

Cited by 6 publications

(3 citation statements)

References 8 publications

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“…Fatty acid methyl esters of which the number of carbon atoms in the chain were 6, 14, and 18 exhibited good results. [3] According to the present work the transesterification activities of the immobilized lipase prepared with the GA-C6, GA-C14 and GA-C18 particles were high. These results agreed with those obtained in the screening.…”

Section: Transesterification Reaction Catalyzed By Immobilized Lipasesupporting

confidence: 60%

“…In our previous article, [3] the transesterification activity of a freeze-dried lipase, which was prepared from Rhizopus chinensis lipase in the presence of a fatty acid methylester or tert-octylphenoxy polyethoxy ethanol (Triton X-100), was considerably high compared to that prepared without additives. This result suggested that these additives improved the solubility and stability of the lipase in nonaqueous solvents.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Synthesis of Amphiphilic Polymer Particles for Lipase Immobilization

Yasuda¹,

Kasahara

Kawahara

et al. 2001

Macromol. Chem. Phys.

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Section: Transesterification Reaction Catalyzed By Immobilized Lipasesupporting

confidence: 60%

Section: Introductionmentioning

confidence: 99%

Synthesis of Amphiphilic Polymer Particles for Lipase Immobilization

Yasuda¹,

Kasahara

Kawahara

et al. 2001

Macromol. Chem. Phys.

Self Cite

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“…Moreover, the treatment of lipase with organic solvents is also one of the effective methods of enzyme modification to improve lipase activity and stability in non-aqueous phase, just as the use of additives, lipid coating, immobilization including covalent attachment and entrapment, and so on [15][16][17][18]. This method is different from the ''solvent engineering'' [19] (organic solvents were used as the reaction medium reported in vast literatures).…”

Section: Introductionmentioning

confidence: 99%

Synthetic activity enhancement of membrane-bound lipase from Rhizopus chinensis by pretreatment with isooctane

Wang

Teng

2007

Bioprocess Biosyst Eng

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The cell-bound lipase from Rhizopus chinensis CCTCC M201021 with high catalysis ability for ester synthesis was located as a membrane-bound lipase by the treatments of Yatalase firstly. In order to improve its synthetic activity in non-aqueous phase, the pretreatments of this enzyme with various organic solvents were investigated. The pretreatment with isooctane improved evidently the lipase synthetic activity, resulting in about 139% in relative synthetic activity and 115% in activity recovery. The morphological changes of mycelia caused by organic solvent pretreatments could influence the exposure of the membrane-bound enzyme from mycelia and the exhibition of the lipase activity. The pretreatment conditions with isooctane and acetone were further investigated, and the optimum effect was obtained by the isooctane pretreatment at 4 degrees C for 1 h, resulting in 156% in relative synthetic activity and 126% in activity recovery. When the pretreated lipases were employed as catalysts for the esterification production of ethyl hexanoate in heptane, higher initial reaction rate and higher final molar conversion were obtained using the lipase pretreated with isooctane, compared with the untreated lyophilized one. This result suggested that the pretreatment of the membrane-bound lipase with isooctane could be an effective method to substitute the lyophilization for preparing biocatalysts used in non-aqueous phase reactions.

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