Change search
Link to record
Permanent link

Direct link
Biundo, Antonino
Publications (3 of 3) Show all publications
Stamm, A., Biundo, A., Schmidt, B., Brücher, J., Lundmark, S., Olsén, P., . . . Syrén, P.-O. (2019). A retrobiosynthesis-based route to generate pinene-derived polyesters. ChemBioChem (Print), 20, 1664-1671
Open this publication in new window or tab >>A retrobiosynthesis-based route to generate pinene-derived polyesters
Show others...
2019 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 20, p. 1664-1671Article in journal (Refereed) Published
Abstract [en]

Significantly increased production of biobased polymers is aprerequisite to replace petroleum-based materials towardsreaching a circular bioeconomy. However, many renewablebuilding blocks from wood and other plant material are notdirectly amenable for polymerization, due to their inert backbonesand/or lack of functional group compatibility with thedesired polymerization type. Based on a retro-biosyntheticanalysis of polyesters, a chemoenzymatic route from (@)-apinenetowards a verbanone-based lactone, which is furtherused in ring-opening polymerization, is presented. Generatedpinene-derived polyesters showed elevated degradation andglass transition temperatures, compared with poly(e-decalactone),which lacks a ring structure in its backbone. Semirationalenzyme engineering of the cyclohexanone monooxygenasefrom Acinetobacter calcoaceticus enabled the biosynthesis ofthe key lactone intermediate for the targeted polyester. As aproof of principle, one enzyme variant identified from screeningin a microtiter plate was used in biocatalytic upscaling,which afforded the bicyclic lactone in 39% conversion in shakeflask scale reactions.

National Category
Polymer Chemistry
Research subject
urn:nbn:se:kth:diva-260797 (URN)10.1002/cbic.201900046 (DOI)000477916100008 ()30793830 (PubMedID)2-s2.0-85066903140 (Scopus ID)

QC 20191008

Available from: 2019-09-30 Created: 2019-09-30 Last updated: 2020-03-09Bibliographically approved
Malmström, E., Fogelström, L., Stamm, A., Tengdelius, M., Biundo, A. & Syrén, P.-O. (2019). Sustainable terpene-based polymeric materials. Paper presented at 257th National Meeting of the American-Chemical-Society (ACS), MAR 31-APR 04, 2019, Orlando, FL. Abstracts of Papers of the American Chemical Society, 257
Open this publication in new window or tab >>Sustainable terpene-based polymeric materials
Show others...
2019 (English)In: Abstracts of Papers of the American Chemical Society, ISSN 0065-7727, Vol. 257Article in journal, Meeting abstract (Other academic) Published
Place, publisher, year, edition, pages
American Chemical Society (ACS), 2019
National Category
Other Chemistry Topics
urn:nbn:se:kth:diva-257660 (URN)000478861204618 ()
257th National Meeting of the American-Chemical-Society (ACS), MAR 31-APR 04, 2019, Orlando, FL

QC 20190903

Available from: 2019-09-03 Created: 2019-09-03 Last updated: 2019-09-03Bibliographically approved
Biundo, A., Subagia, R., Maurer, M., Ribitsch, D., Syrén, P.-O. & Guebitz, G. M. (2019). Switched reaction specificity in polyesterases towards amide bond hydrolysis by enzyme engineering. RSC Advances, 9(62), 36217-36226
Open this publication in new window or tab >>Switched reaction specificity in polyesterases towards amide bond hydrolysis by enzyme engineering
Show others...
2019 (English)In: RSC Advances, ISSN 2046-2069, E-ISSN 2046-2069, Vol. 9, no 62, p. 36217-36226Article in journal (Refereed) Published
Abstract [en]

The recalcitrance of plastics like nylon and other polyamides contributes to environmental problems (e.g. microplastics in oceans) and restricts possibilities for recycling. The fact that hitherto discovered amidases (EC 3.5.1. and 3.5.2.) only show no, or low, activity on polyamides currently obstructs biotechnological-assisted depolymerization of man-made materials. In this work, we capitalized on enzyme engineering to enhance the promiscuous amidase activity of polyesterases. Through enzyme design we created a reallocated water network adapted for hydrogen bond formation to synthetic amide backbones for enhanced transition state stabilization in the polyester-hydrolyzing biocatalysts Humicola insolens cutinase and Thermobifida cellulosilytica cutinase 1. This novel concept enabled increased catalytic efficiency towards amide-containing soluble substrates. The afforded enhanced hydrolysis of the amide bond-containing insoluble substrate 3PA 6,6 by designed variants was aligned with improved transition state stabilization identified by molecular dynamics (MD) simulations. Furthermore, the presence of a favorable water-molecule network that interacted with synthetic amides in the variants resulted in a reduced activity on polyethylene terephthalate (PET). Our data demonstrate the potential of using enzyme engineering to improve the amidase activity for polyesterases to act on synthetic amide-containing polymers.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2019
Thermobifida-Cellulosilytica, Polyethylene Terephthalate, Surface Hydrolysis, Transition-State, Cutinase, Binding, Degradation, Polyethyleneterephthalate, Parameterization, Microplastics
National Category
Chemical Sciences
urn:nbn:se:kth:diva-265458 (URN)10.1039/c9ra07519d (DOI)000497825500036 ()2-s2.0-85075004406 (Scopus ID)

QC 20191213

Available from: 2019-12-13 Created: 2019-12-13 Last updated: 2019-12-13Bibliographically approved

Search in DiVA

Show all publications