Setting of Surimi Paste in Which Transglutaminase Is Inactivated by <i>N</i>-Ethylmaleimide
-
- Nowsad Alam AKM
- Faculty of Bioresources, Mie University
-
- Kanoh Satoshi
- Faculty of Bioresources, Mie University
-
- Niwa Eiji
- Faculty of Bioresources, Mie University
Bibliographic Information
- Other Title
-
- Setting of Surimi Paste in Which Transglutaminase Is Inactivated by N-Ethylmaleimide
- Setting of Surimi Paste in Which Transg
Search this article
Abstract
The effects of N-ethylmaleimide (NEM), a powerful SH reagent, and N-ethylsuccinimide (NES), not an SH reagent but an analogue of the former, on the physico-chemical properties of suwari gel from Alaska pollack surimi were investigated in order to clarify the effect of transglutaminase (TGase) on the setting of surimi paste. TGase was completely inactivated by the addition of more than 0.075% NEM to the paste, but the suwari gel was formed at 30°C even from such a paste. By the addition of this amount of NEM, the breaking force and SH content of muscle proteins decreased to about 65 and 60%, respectively, and the polymerization of myosin heavy chain (MHC) to crosslinked myosin heavy chain (CMHC) was suppressed. On the contrary, the addition of the same amount of NES did not influence the breaking force, SH content, or polymerization of MHC. These findings suggest that the gelation of the paste and the polymerization of MHC occur during setting even in the absence of TGase and that the combined contribution of the formation of CMHC and that of the SS bond to the breaking force of the suwari gel is about 35%.
Journal
-
- Fisheries science
-
Fisheries science 60 (2), 189-191, 1994
The Japanese Society of Fisheries Science
- Tweet
Details 詳細情報について
-
- CRID
- 1390282679404774784
-
- NII Article ID
- 130003741876
- 40005348168
-
- NII Book ID
- AA10993718
-
- NDL BIB ID
- 3641447
-
- ISSN
- 09199268
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- NDL
- Crossref
- CiNii Articles
-
- Abstract License Flag
- Disallowed