Thiol-functionalization of acrylic ester monomers catalyzed by immobilized Humicola insolens cutinase

Kazenwadel, Christian; Eiben, Sabine; Maurer, Steffen; Beuttler, Holger; Wetzl, Dennis; Hauer, Bernhard; Koschorreck, Katja

doi:10.1016/j.enzmictec.2012.03.007

Cited by 13 publications

(5 citation statements)

References 36 publications

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“…insolens expressed in P. pastoris) [63]. On the other hand, bacterial thermophilic cutinases from T. fusca expressed in E. coli BL21, showed an optimal enzyme activity at 55-60 ο C [45,64].…”

Section: Effect Of Temperature and Ph On Activity Of Focut5amentioning

confidence: 99%

Structural and functional studies of a Fusarium oxysporum cutinase with polyethylene terephthalate modification potential

Dimarogona

Nikolaivits

Kanelli

et al. 2015

Biochimica et Biophysica Acta (BBA) - General Subjects

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Section: Effect Of Temperature and Ph On Activity Of Focut5amentioning

confidence: 99%

Structural and functional studies of a Fusarium oxysporum cutinase with polyethylene terephthalate modification potential

Dimarogona

Nikolaivits

Kanelli

et al. 2015

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…Furthermore, heat tolerance is positively associated with other kinds of protein stability, such as tolerance in organic solvents [70], which is also an important property for cutinases that are utilized for synthetic chemistry applications. There are only a few heat-stable cutinases characterized so far, and they all originate from thermophilic microorganisms, such as T. fusca [43], H. insolens [49], and M. cinnamomea [51] (Table 1). Nevertheless, not all cutinases from thermophilic sources have proven to be thermostable, for example, MtCUT from M. thermophila [52].…”

Section: Improving the Heat And Operational Stability Of Cutinasesmentioning

confidence: 99%

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

et al. 2018

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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.

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“…These biotransformations can be used for polyester surface modifications (Eberl et al, ; Gübitz and Paulo, ; Lee and Song, ; Vertommen et al, ; Zhang et al, ) and may provide mild routes for the recycling of commodity polyesters to their corresponding monomers (Barth et al, ; Wei et al, ). Cutinases have also shown utility in small molecule ester synthesis (De Barros et al, , ) and transesterification reactions (Badenes et al, ; Carvalho et al, ; Kazenwadel et al, ).…”

Section: Introductionmentioning

confidence: 99%

Comparative thermal inactivation analysis of Aspergillus oryzae and Thiellavia terrestris cutinase: Role of glycosylation

Shirke

Jones

et al. 2016

Biotech & Bioengineering

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Cutinase thermostability is important so that the enzymes can function above the glass transition of what are often rigid polymer substrates. A detailed thermal inactivation analysis was performed for two well-characterized cutinases, Aspergillus oryzae Cutinase (AoC) and Thiellavia terrestris Cutinase (TtC). Both AoC and TtC are prone to thermal aggregation upon unfolding at high temperature, which was found to be a major reason for irreversible loss of enzyme activity. Our study demonstrates that glycosylation stabilizes TtC expressed in Pichia pastoris by inhibiting its thermal aggregation. Based on the comparative thermal inactivation analyses of non-glycosylated AoC, glycosylated (TtC-G), and non-glycosylated TtC (TtC-NG), a unified model for thermal inactivation is proposed that accounts for thermal aggregation and may be applicable to other cutinase homologues. Inspired by glycosylated TtC, we successfully employed glycosylation site engineering to inhibit AoC thermal aggregation. Indeed, the inhibition of thermal aggregation by AoC glycosylation was greater than that achieved by conventional use of trehalose under a typical condition. Collectively, this study demonstrates the excellent potential of implementing glycosylation site engineering for thermal aggregation inhibition, which is one of the most common reasons for the irreversible thermal inactivation of cutinases and many proteins. Biotechnol. Bioeng. 2017;114: 63-73. © 2016 Wiley Periodicals, Inc.

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Thiol-functionalization of acrylic ester monomers catalyzed by immobilized Humicola insolens cutinase

Cited by 13 publications

References 36 publications

Structural and functional studies of a Fusarium oxysporum cutinase with polyethylene terephthalate modification potential

Structural and functional studies of a Fusarium oxysporum cutinase with polyethylene terephthalate modification potential

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

Comparative thermal inactivation analysis of Aspergillus oryzae and Thiellavia terrestris cutinase: Role of glycosylation

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