Journal
CATALYSTS
Volume 6, Issue 11, Pages -Publisher
MDPI
DOI: 10.3390/catal6110174
Keywords
lipase; adsorption; membrane modification; polyphosphazene; activity
Categories
Funding
- National Natural Science Foundation of China [21274126, 21604032]
- Open Project of Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University [KLIB-KF201501]
- Fundamental Research Funds for the Central Universities [JUSRP51504, JUSRP116031]
- Industry-University-Institute Cooperative Program in Jiangsu Province [BY2015019-37]
- Key Projects in the National Science & Technology Pillar Program [2015BAD15B04]
Ask authors/readers for more resources
In this work, poly(n-butylamino)(allylamino) phosphazene (PBAP) was synthesized and tethered on polypropylene microporous membrane (PPMM) with the aim of offering a biocompatible and, at the same time, moderately hydrophobic microenvironment to lipase for the first time. Lipase from Candida rugosa was used and the influence of membrane surface conditions on the activities of immobilized lipases was evaluated. Water contact angle measurement as well as field emission scanning electron microscopy were used to characterize the morphology of the modified membranes. The results showed an improvement in the adsorption capacity (26.0 mg/m(2)) and activity retention (68.2%) of the immobilized lipases on the PBAP-modified PPMM. Moreover, the lipases immobilized on the modified PPMM showed better thermal and pH stability.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available
Share Paper
