His‐Tag Immobilization of Cutinase 1 From <i>Thermobifida cellulosilytica</i> for Solvent‐Free Synthesis of Polyesters

Pellis, Alessandro; Vastano, Marco; Quartinello, Felice; Acero, Enrique Herrero; Guebitz, Georg M.

doi:10.1002/biot.201700322

Cited by 16 publications

(17 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The immobilized catalyst showed an increase in T opt by 10 • C, and a 2-fold higher t 1/2 at 40 • C. Thc_Cut1 from T. cellulosilytica was ionically bound to Fe(III)-activated carriers taking advantage of its His-tag. The catalyst was capable of being reused up to three times for the synthesis of polybutylene adipate oligomers [84]. Other than chemically synthesized materials, there are some reports of naturally-occurring polysaccharides that have been utilized as immobilization supports.…”

Section: Immobilizationmentioning

confidence: 99%

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

et al. 2018

View full text Add to dashboard Cite

Cutinases are α/β hydrolases, and their role in nature is the degradation of cutin. Such enzymes are usually produced by phytopathogenic microorganisms in order to penetrate their hosts. The first focused studies on cutinases started around 50 years ago. Since then, numerous cutinases have been isolated and characterized, aiming at the elucidation of their structure–function relations. Our deeper understanding of cutinases determines the applications by which they could be utilized; from food processing and detergents, to ester synthesis and polymerizations. However, cutinases are mainly efficient in the degradation of polyesters, a natural function. Therefore, these enzymes have been successfully applied for the biodegradation of plastics, as well as for the delicate superficial hydrolysis of polymeric materials prior to their functionalization. Even though research on this family of enzymes essentially began five decades ago, they are still involved in many reports; novel enzymes are being discovered, and new fields of applications arise, leading to numerous related publications per year. Perhaps the future of cutinases lies in their evolved descendants, such as polyesterases, and particularly PETases. The present article reviews the biochemical and structural characteristics of cutinases and cutinase-like hydrolases, and their applications in the field of bioremediation and biocatalysis.

show abstract

Section: Immobilizationmentioning

confidence: 99%

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

et al. 2018

View full text Add to dashboard Cite

show abstract

“…Regarding HiC, Feder and Gross (2010) investigated polycondensations of different linear diacids and various diols using this enzyme immobilized on Amberzyme oxirane resin at 70 • C, leading to the conclusion that HiC expresses its preference towards long-chain compounds, observing a M n of 6600 Da using dimethyl sebacate and 1,8-octanediol [22]. On the other hand, Thc_Cut1 showed a substrate preference for C 4 -C 6 diesters and diols at 50 • C when immobilized using a His-tag method on different carriers (opal, coral, and amber beads), resulting in a polyester with a molecular weight of 900 Da (M w ) [23]. Higher M w (~1900 Da) was obtained using the biocatalyst covalently immobilized on epoxy resins [6].…”

Section: Introductionmentioning

confidence: 99%

Biocatalyzed Synthesis of Flavor Esters and Polyesters: A Design of Experiments (DoE) Approach

Fabbri

Bertolini

Guebitz

et al. 2021

IJMS

Self Cite

View full text Add to dashboard Cite

In the present work, different hydrolases were adsorbed onto polypropylene beads to investigate their activity both in short-esters and polyesters synthesis. The software MODDE® Pro 13 (Sartorius) was used to develop a full-factorial design of experiments (DoE) to analyse the thermostability and selectivity of the immobilized enzyme towards alcohols and acids with different chain lengths in short-esters synthesis reactions. The temperature optima of Candida antarctica lipase B (CaLB), Humicola insolens cutinase (HiC), and Thermobifida cellulosilytica cutinase 1 (Thc_Cut1) were 85 °C, 70 °C, and 50 °C. CaLB and HiC preferred long-chain alcohols and acids as substrate in contrast to Thc_Cut1, which was more active on short-chain monomers. Polymerization of different esters as building blocks was carried out to confirm the applicability of the obtained model on larger macromolecules. The selectivity of both CaLB and HiC was investigated and best results were obtained for dimethyl sebacate (DMSe), leading to polyesters with a Mw of 18 kDa and 6 kDa. For the polymerization of dimethyl adipate (DMA) with BDO and ODO, higher molecular masses were obtained when using CaLB onto polypropylene beads (CaLB_PP) as compared with CaLB immobilized on macroporous acrylic resin beads (i.e., Novozym 435). Namely, for BDO the Mn were 7500 and 4300 Da and for ODO 8100 and 5000 Da for CaLB_PP and for the commercial enzymes, respectively. Thc_Cut1 led to polymers with lower molecular masses, with Mn < 1 kDa. This enzyme showed a temperature optimum of 50 °C with 63% of DMA and BDO when compared to 54% and 27%, at 70 °C and at 85 °C, respectively.

show abstract

“…Based on previous reports on enzymatic polymerizations conducted using CaLB as biocatalyst, two different approaches were used, and herein, they will be referred to as (A) bulk reaction without solvent, until now only reported for aliphatic monomers 28,29 and (B) reactions in organic media, a traditional reaction system for the enzymatic polycondensation of aromatic moieties 30,31 .…”

Section: Resultsmentioning

confidence: 99%

Enzymatic synthesis of lignin derivable pyridine based polyesters for the substitution of petroleum derived plastics

et al. 2019

Self Cite

View full text Add to dashboard Cite

Following concerns over increasing global plastic pollution, interest in the production and characterization of bio-based and biodegradable alternatives is rising. In the present work, the synthesis of a series of fully bio-based alternatives based on 2,4-, 2,5-, and 2,6-pyridinedicarboxylic acid-derived polymers produced via enzymatic catalysis are reported. A similar series of aromatic-aliphatic polyesters based on diethyl-2,5-furandicarboxylate and of the petroleum-based diethyl terephthalate and diethyl isophthalate were also synthesized. Here we show that the enzymatic synthesis starting from 2,4-diethyl pyridinedicarboxylate leads to the best polymers in terms of molecular weights (M n = 14.3 and M w of 32.1 kDa when combined with 1,8-octanediol) when polymerized in diphenyl ether. Polymerization in solventless conditions were also successful leading to the synthesis of bio-based oligoesters that can be further functionalized. DSC analysis show a clear similarity in the thermal behavior between 2,4-diethyl pyridinedicarboxylate and diethyl isophthalate (amorphous polymers) and between 2,5-diethyl pyridinedicarboxylate and diethyl terephthalate (crystalline polymers).

show abstract

His‐Tag Immobilization of Cutinase 1 From Thermobifida cellulosilytica for Solvent‐Free Synthesis of Polyesters

Cited by 16 publications

References 31 publications

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

Biocatalyzed Synthesis of Flavor Esters and Polyesters: A Design of Experiments (DoE) Approach

Enzymatic synthesis of lignin derivable pyridine based polyesters for the substitution of petroleum derived plastics

Contact Info

Product

Resources

About