Effect of organic solvent on enzymatic degradation of cyclic PBS-based polymers by lipase N435.
Int J Biol Macromol
; 137: 215-223, 2019 Sep 15.
Article
in En
| MEDLINE
| ID: mdl-31255620
ABSTRACT
Poly(butylene succinate-co-cyclohexane dimethanol succinate) (P(BS-co-CHDMS)) and poly(butylene succinate-co-butanediol cyclohexanedicarboxylic acid) (P(BS-co-BCHDA)) were catalytically degraded by Candida antarctica lipase Novozyme 435 (N435) in CHCl3 and THF. The results indicated that the degradation rate was P(BS-co-CHDMS)â¯>â¯P(BS-co-BCHDA)â¯>â¯poly(butylene succinate) (PBS). The degradation rate of copolyesters was higher in CHCl3 than in THF, the highest degradation rate of 67% being obtained for P(BS-co-CHDMS). Hence, the CHCl3 solvent is more suitable for the enzyme-catalytic degradation of copolyesters, since the lipase can easier recognize the butylene succinate (BS-), (butanediol cyclohexanedicarboxylic acid) (BCA-), and (cyclohexane dimethanol succinate-type) (CMS-type) ester bonds in this solvent. Moreover, it can recognize the CMS-type ester bonds with a higher specificity than the (butanediol cyclohexanedicarboxylic acid type) (BCA-type) ester bonds. Molecular simulation results indicated that the structure of the lipase was stable in CHCl3 and THF. However, CHCl3 proved to be more suitable for a stable activity of the enzyme. The active pocket contains acyl-binding hydrophilic residues which are recognized by the substrate. The increase in the content of saturated cycles can increase the hydrophobicity of the substrate and thus, the amount of substrate bond to enzyme active site is increased, which facilitates the enzymatic degradation of copolyesters.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Polyesters
/
Solvents
/
Lipase
Language:
En
Journal:
Int J Biol Macromol
Year:
2019
Document type:
Article