Effect of novel cutinase CcCut1 in degrading potato suberin and berry cutin

Riikka Järvinen, Ulla Holopainen, Antti Nyyssölä, Armando Silvestre, Ana Maria Gil, Pekka Lehtinen, Johanna Buchert, Heikki Kallio

Research output: Contribution to conferenceConference AbstractScientific

Abstract

Cutinases catalyze the hydrolysis of natural cuticular polyesters (cutin, suberin) tolower molecular weight components. These enzymes are thus potentially valuabletools for by-product exploitation in agricultural industry. Cutin and suberin polymers are composed of long chain non-substituted and hydroxy/epoxy-substituted ? hydroxy fatty acids and a,?-dicarboxylic acids. A novel cutinase CcCUT1 (from Coprinus cinereus) was investigated for degradation of potato suberin and black currant cutin. Cutinase hydrolysis and chemical methanolysis of suberin were compared and the CHCl3-soluble monomeric fragments identified as TMS derivatives with GC-MS. The solid, hydrolysis-resistant residues of suberin were analyzed with solid state 13C CP-MAS NMR and FT-IR. The cutinase hydrolysis resistant residual microstructures, of both potato suberin and black currant cutin, were analysed by light and confocal microscopy. Gravimetrical analysis showed that methanolysis was more effective than cutinase treatment for releasing CHCl3-soluble material. The results of the analysis of monomeric components indicate that cutinases are more specific towards a,?-dioic acids than ?-hydroxy acids. Spectroscopic analysis and microscopy of the residues further revealed the mode of action.
Original languageEnglish
Publication statusPublished - 2010
MoE publication typeNot Eligible
Event240th ACS National Meeting and Exposition - Boston, United States
Duration: 22 Aug 201026 Aug 2010

Conference

Conference240th ACS National Meeting and Exposition
CountryUnited States
CityBoston
Period22/08/1026/08/10

Fingerprint

Hydrolysis
Dicarboxylic Acids
Hydroxy Acids
Polyesters
Spectroscopic analysis
Confocal microscopy
Optical microscopy
Byproducts
cutinase
cutin
suberin
Microscopic examination
Polymers
Fatty Acids
Molecular weight
Nuclear magnetic resonance
Derivatives
Degradation
Microstructure
Acids

Cite this

Järvinen, R., Holopainen, U., Nyyssölä, A., Silvestre, A., Gil, A. M., Lehtinen, P., ... Kallio, H. (2010). Effect of novel cutinase CcCut1 in degrading potato suberin and berry cutin. Abstract from 240th ACS National Meeting and Exposition, Boston, United States.
Järvinen, Riikka ; Holopainen, Ulla ; Nyyssölä, Antti ; Silvestre, Armando ; Gil, Ana Maria ; Lehtinen, Pekka ; Buchert, Johanna ; Kallio, Heikki. / Effect of novel cutinase CcCut1 in degrading potato suberin and berry cutin. Abstract from 240th ACS National Meeting and Exposition, Boston, United States.
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abstract = "Cutinases catalyze the hydrolysis of natural cuticular polyesters (cutin, suberin) tolower molecular weight components. These enzymes are thus potentially valuabletools for by-product exploitation in agricultural industry. Cutin and suberin polymers are composed of long chain non-substituted and hydroxy/epoxy-substituted ? hydroxy fatty acids and a,?-dicarboxylic acids. A novel cutinase CcCUT1 (from Coprinus cinereus) was investigated for degradation of potato suberin and black currant cutin. Cutinase hydrolysis and chemical methanolysis of suberin were compared and the CHCl3-soluble monomeric fragments identified as TMS derivatives with GC-MS. The solid, hydrolysis-resistant residues of suberin were analyzed with solid state 13C CP-MAS NMR and FT-IR. The cutinase hydrolysis resistant residual microstructures, of both potato suberin and black currant cutin, were analysed by light and confocal microscopy. Gravimetrical analysis showed that methanolysis was more effective than cutinase treatment for releasing CHCl3-soluble material. The results of the analysis of monomeric components indicate that cutinases are more specific towards a,?-dioic acids than ?-hydroxy acids. Spectroscopic analysis and microscopy of the residues further revealed the mode of action.",
author = "Riikka J{\"a}rvinen and Ulla Holopainen and Antti Nyyss{\"o}l{\"a} and Armando Silvestre and Gil, {Ana Maria} and Pekka Lehtinen and Johanna Buchert and Heikki Kallio",
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Järvinen, R, Holopainen, U, Nyyssölä, A, Silvestre, A, Gil, AM, Lehtinen, P, Buchert, J & Kallio, H 2010, 'Effect of novel cutinase CcCut1 in degrading potato suberin and berry cutin' 240th ACS National Meeting and Exposition, Boston, United States, 22/08/10 - 26/08/10, .

Effect of novel cutinase CcCut1 in degrading potato suberin and berry cutin. / Järvinen, Riikka; Holopainen, Ulla; Nyyssölä, Antti; Silvestre, Armando; Gil, Ana Maria; Lehtinen, Pekka; Buchert, Johanna; Kallio, Heikki.

2010. Abstract from 240th ACS National Meeting and Exposition, Boston, United States.

Research output: Contribution to conferenceConference AbstractScientific

TY - CONF

T1 - Effect of novel cutinase CcCut1 in degrading potato suberin and berry cutin

AU - Järvinen, Riikka

AU - Holopainen, Ulla

AU - Nyyssölä, Antti

AU - Silvestre, Armando

AU - Gil, Ana Maria

AU - Lehtinen, Pekka

AU - Buchert, Johanna

AU - Kallio, Heikki

PY - 2010

Y1 - 2010

N2 - Cutinases catalyze the hydrolysis of natural cuticular polyesters (cutin, suberin) tolower molecular weight components. These enzymes are thus potentially valuabletools for by-product exploitation in agricultural industry. Cutin and suberin polymers are composed of long chain non-substituted and hydroxy/epoxy-substituted ? hydroxy fatty acids and a,?-dicarboxylic acids. A novel cutinase CcCUT1 (from Coprinus cinereus) was investigated for degradation of potato suberin and black currant cutin. Cutinase hydrolysis and chemical methanolysis of suberin were compared and the CHCl3-soluble monomeric fragments identified as TMS derivatives with GC-MS. The solid, hydrolysis-resistant residues of suberin were analyzed with solid state 13C CP-MAS NMR and FT-IR. The cutinase hydrolysis resistant residual microstructures, of both potato suberin and black currant cutin, were analysed by light and confocal microscopy. Gravimetrical analysis showed that methanolysis was more effective than cutinase treatment for releasing CHCl3-soluble material. The results of the analysis of monomeric components indicate that cutinases are more specific towards a,?-dioic acids than ?-hydroxy acids. Spectroscopic analysis and microscopy of the residues further revealed the mode of action.

AB - Cutinases catalyze the hydrolysis of natural cuticular polyesters (cutin, suberin) tolower molecular weight components. These enzymes are thus potentially valuabletools for by-product exploitation in agricultural industry. Cutin and suberin polymers are composed of long chain non-substituted and hydroxy/epoxy-substituted ? hydroxy fatty acids and a,?-dicarboxylic acids. A novel cutinase CcCUT1 (from Coprinus cinereus) was investigated for degradation of potato suberin and black currant cutin. Cutinase hydrolysis and chemical methanolysis of suberin were compared and the CHCl3-soluble monomeric fragments identified as TMS derivatives with GC-MS. The solid, hydrolysis-resistant residues of suberin were analyzed with solid state 13C CP-MAS NMR and FT-IR. The cutinase hydrolysis resistant residual microstructures, of both potato suberin and black currant cutin, were analysed by light and confocal microscopy. Gravimetrical analysis showed that methanolysis was more effective than cutinase treatment for releasing CHCl3-soluble material. The results of the analysis of monomeric components indicate that cutinases are more specific towards a,?-dioic acids than ?-hydroxy acids. Spectroscopic analysis and microscopy of the residues further revealed the mode of action.

M3 - Conference Abstract

ER -

Järvinen R, Holopainen U, Nyyssölä A, Silvestre A, Gil AM, Lehtinen P et al. Effect of novel cutinase CcCut1 in degrading potato suberin and berry cutin. 2010. Abstract from 240th ACS National Meeting and Exposition, Boston, United States.