Modification of wheat gluten with oxidative enzymes

Sari Virtanen, Karin Autio, Maija Tenkanen, Marja-Leena Niku-Paavola

Research output: Chapter in Book/Report/Conference proceedingConference article in proceedingsScientificpeer-review

1 Citation (Scopus)

Abstract

Conventional enzymatic treatments in food processing are performed by using hydrolytic enzymes. The utilization of other types of enzymes, such as transglutaminase or oxidative enzymes, is continuously increasing. Transglutaminase (EC 2.3.2.13) catalyzes the reaction between glutamine and e.g lysine residues and creates new peptide linkages into and between the polypeptide chains of proteins. Oxidoreductases, like monophenol monooxygenase (EC 1.14.18.1), catechol oxidase (EC 1.10.3.1) and laccase (EC 1.10.3.2) may also modify proteins. Monophenol monooxygenase, tyrosinase, is known to act on tyrosine. It could be assumed that phenoloxidases may attack also other aromatic amino acids. VTT Biotechnology and Food Research has worked with laccases for several years and developed applications for different purposes. Applications in pulp and paper, textile, and chemical industry have been successful. Laccase is an ideal enzyme because it does not need any co-factors and it is active towards a variety of structurally different substrates. Laccase starts a radical reaction resulting polymerization. Concerning proteins this may include cross-linking. It has been reported recently that treatment with laccase improves the baking quality of flour (1). The aim here was to study the effects of laccases on the proteins of wheat gluten fraction.
Original languageEnglish
Title of host publication2nd European Symposium on Enzymes in Grain Processing, ESEPG-2
Place of PublicationEspoo
PublisherVTT Technical Research Centre of Finland
Pages299-304
ISBN (Electronic)951-38-5707-7
ISBN (Print)951-38-5706-9
Publication statusPublished - 2000
MoE publication typeA4 Article in a conference publication
EventEuropean Symposium on Enzymes in Grain Processing, ESEGP-2 - Helsinki, Finland
Duration: 8 Dec 199910 Dec 1999

Publication series

NameVTT Symposium
PublisherVTT
Number207
ISSN (Print)0357-9387
ISSN (Electronic)1455-0873

Conference

ConferenceEuropean Symposium on Enzymes in Grain Processing, ESEGP-2
Abbreviated titleESEGP-2
CountryFinland
CityHelsinki
Period8/12/9910/12/99

Fingerprint

wheat gluten
laccase
enzymes
protein-glutamine gamma-glutamyltransferase
monophenol monooxygenase
catechol oxidase
proteins
baking quality
food research
pulp and paper industry
chemical industry
textile industry
enzymatic treatment
oxidoreductases
crosslinking
food processing
glutamine
polymerization
biotechnology
linkage (genetics)

Cite this

Virtanen, S., Autio, K., Tenkanen, M., & Niku-Paavola, M-L. (2000). Modification of wheat gluten with oxidative enzymes. In 2nd European Symposium on Enzymes in Grain Processing, ESEPG-2 (pp. 299-304). Espoo: VTT Technical Research Centre of Finland. VTT Symposium, No. 207
Virtanen, Sari ; Autio, Karin ; Tenkanen, Maija ; Niku-Paavola, Marja-Leena. / Modification of wheat gluten with oxidative enzymes. 2nd European Symposium on Enzymes in Grain Processing, ESEPG-2. Espoo : VTT Technical Research Centre of Finland, 2000. pp. 299-304 (VTT Symposium; No. 207).
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title = "Modification of wheat gluten with oxidative enzymes",
abstract = "Conventional enzymatic treatments in food processing are performed by using hydrolytic enzymes. The utilization of other types of enzymes, such as transglutaminase or oxidative enzymes, is continuously increasing. Transglutaminase (EC 2.3.2.13) catalyzes the reaction between glutamine and e.g lysine residues and creates new peptide linkages into and between the polypeptide chains of proteins. Oxidoreductases, like monophenol monooxygenase (EC 1.14.18.1), catechol oxidase (EC 1.10.3.1) and laccase (EC 1.10.3.2) may also modify proteins. Monophenol monooxygenase, tyrosinase, is known to act on tyrosine. It could be assumed that phenoloxidases may attack also other aromatic amino acids. VTT Biotechnology and Food Research has worked with laccases for several years and developed applications for different purposes. Applications in pulp and paper, textile, and chemical industry have been successful. Laccase is an ideal enzyme because it does not need any co-factors and it is active towards a variety of structurally different substrates. Laccase starts a radical reaction resulting polymerization. Concerning proteins this may include cross-linking. It has been reported recently that treatment with laccase improves the baking quality of flour (1). The aim here was to study the effects of laccases on the proteins of wheat gluten fraction.",
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Virtanen, S, Autio, K, Tenkanen, M & Niku-Paavola, M-L 2000, Modification of wheat gluten with oxidative enzymes. in 2nd European Symposium on Enzymes in Grain Processing, ESEPG-2. VTT Technical Research Centre of Finland, Espoo, VTT Symposium, no. 207, pp. 299-304, European Symposium on Enzymes in Grain Processing, ESEGP-2, Helsinki, Finland, 8/12/99.

Modification of wheat gluten with oxidative enzymes. / Virtanen, Sari; Autio, Karin; Tenkanen, Maija; Niku-Paavola, Marja-Leena.

2nd European Symposium on Enzymes in Grain Processing, ESEPG-2. Espoo : VTT Technical Research Centre of Finland, 2000. p. 299-304 (VTT Symposium; No. 207).

Research output: Chapter in Book/Report/Conference proceedingConference article in proceedingsScientificpeer-review

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T1 - Modification of wheat gluten with oxidative enzymes

AU - Virtanen, Sari

AU - Autio, Karin

AU - Tenkanen, Maija

AU - Niku-Paavola, Marja-Leena

PY - 2000

Y1 - 2000

N2 - Conventional enzymatic treatments in food processing are performed by using hydrolytic enzymes. The utilization of other types of enzymes, such as transglutaminase or oxidative enzymes, is continuously increasing. Transglutaminase (EC 2.3.2.13) catalyzes the reaction between glutamine and e.g lysine residues and creates new peptide linkages into and between the polypeptide chains of proteins. Oxidoreductases, like monophenol monooxygenase (EC 1.14.18.1), catechol oxidase (EC 1.10.3.1) and laccase (EC 1.10.3.2) may also modify proteins. Monophenol monooxygenase, tyrosinase, is known to act on tyrosine. It could be assumed that phenoloxidases may attack also other aromatic amino acids. VTT Biotechnology and Food Research has worked with laccases for several years and developed applications for different purposes. Applications in pulp and paper, textile, and chemical industry have been successful. Laccase is an ideal enzyme because it does not need any co-factors and it is active towards a variety of structurally different substrates. Laccase starts a radical reaction resulting polymerization. Concerning proteins this may include cross-linking. It has been reported recently that treatment with laccase improves the baking quality of flour (1). The aim here was to study the effects of laccases on the proteins of wheat gluten fraction.

AB - Conventional enzymatic treatments in food processing are performed by using hydrolytic enzymes. The utilization of other types of enzymes, such as transglutaminase or oxidative enzymes, is continuously increasing. Transglutaminase (EC 2.3.2.13) catalyzes the reaction between glutamine and e.g lysine residues and creates new peptide linkages into and between the polypeptide chains of proteins. Oxidoreductases, like monophenol monooxygenase (EC 1.14.18.1), catechol oxidase (EC 1.10.3.1) and laccase (EC 1.10.3.2) may also modify proteins. Monophenol monooxygenase, tyrosinase, is known to act on tyrosine. It could be assumed that phenoloxidases may attack also other aromatic amino acids. VTT Biotechnology and Food Research has worked with laccases for several years and developed applications for different purposes. Applications in pulp and paper, textile, and chemical industry have been successful. Laccase is an ideal enzyme because it does not need any co-factors and it is active towards a variety of structurally different substrates. Laccase starts a radical reaction resulting polymerization. Concerning proteins this may include cross-linking. It has been reported recently that treatment with laccase improves the baking quality of flour (1). The aim here was to study the effects of laccases on the proteins of wheat gluten fraction.

M3 - Conference article in proceedings

SN - 951-38-5706-9

T3 - VTT Symposium

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BT - 2nd European Symposium on Enzymes in Grain Processing, ESEPG-2

PB - VTT Technical Research Centre of Finland

CY - Espoo

ER -

Virtanen S, Autio K, Tenkanen M, Niku-Paavola M-L. Modification of wheat gluten with oxidative enzymes. In 2nd European Symposium on Enzymes in Grain Processing, ESEPG-2. Espoo: VTT Technical Research Centre of Finland. 2000. p. 299-304. (VTT Symposium; No. 207).