The Effect of Different Matrix Bound on the Transesterification Activity of Immobilized PPD2 Lipase
Immobilization of thermostable lipase from Geobacillus thermoleovorans PPD2 (Lip-A) were carried out on Ni-NTA agarose and carboxymethyl chitosan. Free enzyme was obtained by heterologous expression in Escherichia coli as a host cell. The enzyme showed catalytic activity for transesterification reac...
Main Authors: | , , , |
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Format: | Article |
Language: | English |
Published: |
Journal of Pure and Applied Microbiology
2018-06-01
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Series: | Journal of Pure and Applied Microbiology |
Subjects: | |
Online Access: | https://microbiologyjournal.org/the-effect-of-different-matrix-bound-on-the-transesterification-activity-of-immobilized-ppd2-lipase/ |
Summary: | Immobilization of thermostable lipase from Geobacillus thermoleovorans PPD2 (Lip-A) were carried out on Ni-NTA agarose and carboxymethyl chitosan. Free enzyme was obtained by heterologous expression in Escherichia coli as a host cell. The enzyme showed catalytic activity for transesterification reaction. Transesterification activity of immobilized lipase on Ni-NTA agarose was increased by three fold (75.04% conversion) compared to that the free enzyme (24.65%), while the activity of immobilized lipase on carboxymethyl chitosan was slightly decreased (19.86%).
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ISSN: | 0973-7510 2581-690X |