Poly(3-hydroxyoctanoate) depolymerase from Pseudomonas fluorescens GK13: Catalysis of ester-forming reactions in non-aqueous media

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• 作者：Marta Santos^a ; ¹ ; Joana Gangoiti^a ; ¹ ; Marí ; a J. Llama^a ; Juan L. Serra^a ; Helmut Keul^b ; ^{keul@dwi.rwth-aachen.de} ; Martin Mö ; ller^b
• 关键词：Pseudomonas fluorescens GK13 ; Extracellular mcl-PHA depolymerase ; Enzymatic ring-opening polymerization ; Novozyme 435
• 刊名：Journal of Molecular Catalysis B: Enzymatic
• 出版年：2012
• 出版时间：May, 2012
• 年：2012
• 卷：77
• 期：Complete
• 页码：81-86
• 全文大小：291 K

文摘

Several industrial processes based on lipase catalysis have been established. However, since there are still a vast number of catalytic processes that lack a suitable enzyme, the discovery of new biocatalysts is required to fulfil this purpose. The potential of using the medium-chain-length (mcl)-PHA depolymerase from Pseudomonas fluorescens GK13 in anhydrous media to catalyze ester-forming reactions has been investigated and compared with that of Novozyme 435. The mcl-PHA depolymerase catalyzes the ring-opening polymerization of racemic ¦Â-butyrolactone (¦Â-BL), l- and d-lactide (LLA, DLA) with high yield resulting in low molecular weight polymers. On the other hand, ?-caprolactone and pentadecalactone, which show high polymerizability using Novozyme 435 as catalyst, were not polymerized by mcl-PHA depolymerase. Besides, the activity of mcl-PHA depolymerase toward transesterification and esterification of ethyl-3-hydroxyoctanoate, lauric acid, (R,S)-¦Â-BL, LLA and DLA has been studied.