Relationship between Enzyme Adsorption and Enzyme‐Catalyzed Degradation of Polylactides
Abstract
The adsorption of proteinase K on PLLA and PDLA films was studied by CA, surface tension, and microscopic measurements. ESEM clearly shows that proteinase K can irreversibly adsorb on PLLA film. In contrast, no enzyme adsorption was detected on PDLA film under the same conditions. The CA of PLLA film rapidly decreases after immersion in Tris buffer containing proteinase K, whereas that of PDLA remains unchanged. These findings indicate that enzyme adsorption may be a prerequisite for enzymatic degradation of polylactide substrates. Surface tension measurements allow calculation of the average area occupied per proteinase K molecule. The results show that the enzyme molecules exhibit a more compact conformation at higher temperature. magnified image
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Wei, Li et al. showed that proteinase K degraded PLLA faster than PDLA, mostly owing to higher adsorption of the enzyme at the surface of PLLA as compared to PDLA.
“However, Wei, Li et al. showed that proteinase K degraded PLLA faster than PDLA, mostly owing to higher adsorption of the enzyme at the surface of PLLA as compared to PDLA.527”
From Catalysis as an Enabling Science for Sustainable Polymers (2018) · cites this paper as [527]
In a study on the influence of PLA chirality on proteinase K degradation activity, LL, DL, and LD diads could be cleaved, but not DD diads.
“In a thorough study on the influence of the chirality of PLA on the degradation activity of proteinase K, they also evidenced that LL, DL, and LD diads could be cleaved, but not DD diads.”
From Catalysis as an Enabling Science for Sustainable Polymers (2018) · cites this paper as [527]
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- Authors
- Zhao, Z., Yang, L., Hua, J., Wei, J., Gachet, S., Ghzaoui, A. E., & Li, S.
- Affiliations
- Fudan University (CN)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Wei, Jia
- Li, Suming
- ORCID
- Venue
- Macromolecular Bioscience
- Publisher
- Wiley
- Published
- 2007-12-21
- Volume
- 8
- Issue
- 1
- Pages
- 25-31
- ISSN
- 1616-5187 (ISSN-L)
- 1616-5195
- OpenAlex
- W2113581490
- Cited by
- 25
- References
- 19
- Citations by year
- 2026: 1 · 2025: 2 · 2022: 2 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 2 · 2015: 2 · 2014: 2 · 2012: 1
- FWCI
- 1.69
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Macromolecular Bioscience (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Physical Sciences › Materials Science › Biomaterials › biodegradable polymer synthesis and properties
- Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Keywords
- enzyme adsorption, proteinase K, polylactic acid, polycaprolactone, enzymatic degradation, contact angle, surface tension, enzyme conformation, temperature dependence, irreversible adsorption
- MeSH terms
- Adsorption, Chromatography, Gel, Microscopy, Electron, Scanning, Polyesters, Surface Tension, X-Ray Diffraction, Endopeptidase K
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