Role of transglutaminase-mediated cross-linking of protein in the temperature-dependent setting of Alaska pollack surimi
During the low temperature setting of fish paste, myosin heavy chain (MHC) is polymerized to cross-linked myosin heavy chain (CMHC), which is considered to occur by the action of endogenous transglutaminase (TGase). In this study the contribution of TGase on the setting of Alaska pollack surimi at different temperatures was studied. Alaska pollack surimi was ground with 3% NaCl, 30% h2o and with or without ethylene glycol bis (β-aminoethylether) N, N, N¹,N¹- tetra acetic acid (EGTA), an inhibitor of TGase. Among the pastes without EGTA, highest TGase activity was observed at 25°C but breaking force of the gel set at 25°C was lower than that set at 30°, 35°, and 40°C. Addition of EGTA (5m mol/kg) to the paste suppressed TGase activity at all setting temperatures from 20° to 40°C. Gelation of the pastes and cross-linking of MHC on addition of EGTA were suppressed completely at 20° and 25°C, partially at 30° and 35°C, and not at all at 40°C. The findings suggested that during the setting of Alaska pollack surimi TGase mediated cross-linking of MHC was strong at around 25°C but the thermal aggregation of MHC by non-covalent bonds was strong at above 35°C. Setting of surimi at 40°C and cross-linking of its MHC did not involve TGase.
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Language: | English |
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1997
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Subjects: | Fisheries, surimi, transglutaminase, myosin heavy chain, processing fishery products, |
Online Access: | http://hdl.handle.net/1834/32207 |
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dig-aquadocs-1834-322072021-07-04T03:52:45Z Role of transglutaminase-mediated cross-linking of protein in the temperature-dependent setting of Alaska pollack surimi Nowsad Alam, A.K.M. Fisheries surimi transglutaminase myosin heavy chain processing fishery products During the low temperature setting of fish paste, myosin heavy chain (MHC) is polymerized to cross-linked myosin heavy chain (CMHC), which is considered to occur by the action of endogenous transglutaminase (TGase). In this study the contribution of TGase on the setting of Alaska pollack surimi at different temperatures was studied. Alaska pollack surimi was ground with 3% NaCl, 30% h2o and with or without ethylene glycol bis (β-aminoethylether) N, N, N¹,N¹- tetra acetic acid (EGTA), an inhibitor of TGase. Among the pastes without EGTA, highest TGase activity was observed at 25°C but breaking force of the gel set at 25°C was lower than that set at 30°, 35°, and 40°C. Addition of EGTA (5m mol/kg) to the paste suppressed TGase activity at all setting temperatures from 20° to 40°C. Gelation of the pastes and cross-linking of MHC on addition of EGTA were suppressed completely at 20° and 25°C, partially at 30° and 35°C, and not at all at 40°C. The findings suggested that during the setting of Alaska pollack surimi TGase mediated cross-linking of MHC was strong at around 25°C but the thermal aggregation of MHC by non-covalent bonds was strong at above 35°C. Setting of surimi at 40°C and cross-linking of its MHC did not involve TGase. 2021-06-24T17:21:09Z 2021-06-24T17:21:09Z 1997 article 1026-6690 http://hdl.handle.net/1834/32207 en application/pdf application/pdf 75-82 http://aquaticcommons.org/id/eprint/16376 12051 2015-03-27 10:20:22 16376 Bangladesh Fisheries Research Institute |
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Fisheries surimi transglutaminase myosin heavy chain processing fishery products Fisheries surimi transglutaminase myosin heavy chain processing fishery products |
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Fisheries surimi transglutaminase myosin heavy chain processing fishery products Fisheries surimi transglutaminase myosin heavy chain processing fishery products Nowsad Alam, A.K.M. Role of transglutaminase-mediated cross-linking of protein in the temperature-dependent setting of Alaska pollack surimi |
description |
During the low temperature setting of fish paste, myosin heavy chain (MHC) is polymerized to cross-linked myosin heavy chain (CMHC), which is considered to occur by the action of endogenous transglutaminase (TGase). In this study the contribution of TGase on the setting of Alaska pollack surimi at different temperatures was studied. Alaska pollack surimi was ground with 3% NaCl, 30% h2o and with or without ethylene glycol bis (β-aminoethylether) N, N, N¹,N¹- tetra acetic acid (EGTA), an inhibitor of TGase. Among the pastes without EGTA, highest TGase activity was observed at 25°C but breaking force of the gel set at 25°C was lower than that set at 30°, 35°, and 40°C. Addition of EGTA (5m mol/kg) to the paste suppressed TGase activity at all setting temperatures from 20° to 40°C. Gelation of the pastes and cross-linking of MHC on addition of EGTA were suppressed completely at 20° and 25°C, partially at 30° and 35°C, and not at all at 40°C. The findings suggested that during the setting of Alaska pollack surimi TGase mediated cross-linking of MHC was strong at around 25°C but the thermal aggregation of MHC by non-covalent bonds was strong at above 35°C. Setting of surimi at 40°C and cross-linking of its MHC did not involve TGase. |
format |
article |
topic_facet |
Fisheries surimi transglutaminase myosin heavy chain processing fishery products |
author |
Nowsad Alam, A.K.M. |
author_facet |
Nowsad Alam, A.K.M. |
author_sort |
Nowsad Alam, A.K.M. |
title |
Role of transglutaminase-mediated cross-linking of protein in the temperature-dependent setting of Alaska pollack surimi |
title_short |
Role of transglutaminase-mediated cross-linking of protein in the temperature-dependent setting of Alaska pollack surimi |
title_full |
Role of transglutaminase-mediated cross-linking of protein in the temperature-dependent setting of Alaska pollack surimi |
title_fullStr |
Role of transglutaminase-mediated cross-linking of protein in the temperature-dependent setting of Alaska pollack surimi |
title_full_unstemmed |
Role of transglutaminase-mediated cross-linking of protein in the temperature-dependent setting of Alaska pollack surimi |
title_sort |
role of transglutaminase-mediated cross-linking of protein in the temperature-dependent setting of alaska pollack surimi |
publishDate |
1997 |
url |
http://hdl.handle.net/1834/32207 |
work_keys_str_mv |
AT nowsadalamakm roleoftransglutaminasemediatedcrosslinkingofproteininthetemperaturedependentsettingofalaskapollacksurimi |
_version_ |
1756078928360898560 |