Characterization of an acidic cold-adapted cutinase from Thielavia terrestris and its application in flavor ester synthesis

Xu, Hui; Yan, Qiaojuan; Duan, Xiaojie; Yang, Shaoqing; Jiang, Zhengqiang

doi:10.1016/j.foodchem.2015.05.026

Cited by 26 publications

(24 citation statements)

References 39 publications

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“…On the contrary, bacterial cutinases have been expressed, as expected, only in E. coli strains, mostly BL21, with very few exceptions [23,24]. Furthermore, only a limited number of cutinases have been isolated and characterized from wild-type (WT) microorganisms, such as Thielavia terrestris [25,26], Cryptococcus magnus [27], Paraphoma sp. [28], Aspergillus oryzae [29], and Aspergillus nidulans [30].…”

Section: Biochemical Characteristicsmentioning

confidence: 96%

“…The molecular weight (MW) of fungal cutinases ranges from 20 to 25 kDa, with very few exceptions, such as THCUT1 from Trichoderma harzianum [31], Acut3-6hp from Arxula adeninivorans [19], ANCUT2 from A. nidulans [30], and TtcutB from T. terrestris [25], with MWs varying between 27.3 and 29.2 kDa. On the other hand, the MW of bacterial cutinases is usually around 30 kDa, with only two characterized enzymes from Thermomonospora curvata exhibiting a higher size of 35 kDa [24].…”

Section: Biochemical Characteristicsmentioning

confidence: 99%

“…As a rule, cutinases work optimally at neutral or alkaline pH (7.0-9.5). However, there are some reports of cutinases that prefer slightly acidic (pH 6) [18,32,33] or acidic (pH 4-5) [19,25,26,34] conditions. Regarding the effect of temperature, bacterial cutinases act optimally at 50-60 • C, probably due to the fact that they all derive from thermophilic sources.…”

Section: Biochemical Characteristicsmentioning

confidence: 99%

“…Chemical synthesis can be cheap, but not environmentally friendly, since the reactions take place at high temperatures of around 150-240 • C. Enzymatically, these compounds can be synthesized by esterification or transesterification reactions of fatty acids, or of their esters and alcohols, in organic solvents at temperatures of 25-50 • C. The mechanism of these reactions follows the Ping Pong Bi model, and suffers from alcohol inhibition [160,161]. The yields for both types of reactions in non-conventional media, such as isooctane or heptane, are high in most cases (>95%) [25,162]. The highest yields for butyl butyrate synthesis have been achieved in isooctane by esterification using cutinase from M. cinnamonea (McCut) (97%) [51], and by transesterification with cutinase from F. oxysporum (imFocut5a) (>99%) [90].…”

Section: Cutinases As a Tool For Synthetic Chemistrymentioning

confidence: 99%

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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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Section: Biochemical Characteristicsmentioning

confidence: 96%

Section: Biochemical Characteristicsmentioning

confidence: 99%

Section: Biochemical Characteristicsmentioning

confidence: 99%

Section: Cutinases As a Tool For Synthetic Chemistrymentioning

confidence: 99%

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

et al. 2018

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“…In addition, butyl esters show interesting properties like a high boiling point, low viscosity, and low temperature behaviors for food and cosmetic industries [38,39]. HaSGNH1 could be suitable for butyl esters production because it prefers short-chain length substrates, and butyl esters have been successfully synthesized by several other lipases [40,41]. As shown in Fig.…”

Section: Synthesis Of Butyl and Oleic Estersmentioning

confidence: 99%

Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus

Yoo

Jeon

et al. 2020

Biotechnol Biofuels

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Background: Biodiesel and flavor compound production using enzymatic transesterification by microbial lipases provides mild reaction conditions and low energy cost compared to the chemical process. SGNH-type lipases are very effective catalysts for enzymatic transesterification due to their high reaction rate, great stability, relatively small size for convenient genetic manipulations, and ease of immobilization. Hence, it is highly important to identify novel SGNH-type lipases with high catalytic efficiencies and good stabilities. Results: A promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from Halocynthiibacter arcticus was catalytically characterized and functionally explored. HaSGNH1 displayed broad substrate specificity that included tert-butyl acetate, glucose pentaacetate, and p-nitrophenyl esters with excellent stability and high efficiency. Important amino acids (N83, M86, R87, F131, and I173F) around the substrate-binding pocket were shown to be responsible for catalytic activity, substrate specificity, and reaction kinetics. Moreover, immobilized HaSGNH1 was used to produce high yields of butyl and oleic esters. Conclusions: This work provides a molecular understanding of substrate specificities, catalytic regulation, immobilization, and industrial applications of a promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from H. arcticus. This is the first analysis on biodiesel and flavor synthesis using a cold-adapted halophilic SGNH-type lipase from a Halocynthiibacter species.

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Expression and characterization of two glucuronoyl esterases from Thielavia terrestris and their application in enzymatic hydrolysis of corn bran

Tang

Long

Cao

et al. 2019

Appl Microbiol Biotechnol

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Characterization of an acidic cold-adapted cutinase from Thielavia terrestris and its application in flavor ester synthesis

Cited by 26 publications

References 39 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

Biodiesel and flavor compound production using a novel promiscuous cold-adapted SGNH-type lipase (HaSGNH1) from the psychrophilic bacterium Halocynthiibacter arcticus

Expression and characterization of two glucuronoyl esterases from Thielavia terrestris and their application in enzymatic hydrolysis of corn bran

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