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Immobilization of cross‐linked lipase aggregates onto magnetic beads for enzymatic degradation of polycaprolactone
Author(s) -
Kim Mina,
Park JaeMin,
Um HyunJu,
Lee DongHun,
Lee KyuHo,
Kobayashi Fumihisa,
Iwasaka Yasunobu,
Hong ChunSang,
Min Jiho,
Kim YangHoon
Publication year - 2010
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.200900099
Subject(s) - lipase , glutaraldehyde , immobilized enzyme , chemistry , polycaprolactone , chromatography , candida rugosa , biodegradation , degradation (telecommunications) , enzyme , organic chemistry , polymer , telecommunications , computer science
Abstract Candida rugosa lipase was immobilized on amino‐functionalized magnetic supports via cross‐linked enzyme aggregates (CLEA) and used to enhance the enzymatic degradation of polycaprolactone (PCL). The maximum amounts of lipase immobilized on the magnetic beads using glutaraldehyde as a coupling agent were determined to be 33.7 mg/g of beads with an 81% recovery of activity after immobilization. Compared to the free enzyme, the immobilized lipase showed the optimum pH at 1 unit higher (pH 8.0) and also retained its enzymatic activity at higher temperatures. There was 62.9% retention of lipase activity after 30 consecutive reuses, indicating its stability and reusability in aqueous media. Moreover, the immobilized lipase maintained more than 80% of its initial activity during 30 days storage period, while the free lipase lost all under same condition. In addition, the immobilized lipase showed a more than 6‐fold increase in biodegradability over the free lipase when the immobilized lipase was used to degrade PCL in a batch system. Higher thermal and storage stability, as well as good durability after repeated use of the immobilized lipase CLEA, highlights its potential applicability as large scale continuous systems for the enzymatic degradation of PCL. (© 2010 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)