In order to clarify the effect of oxidation itself on the gel formation of salted-surimi through setting, the gel-forming properties were examined with or without transglutaminase (TGase) inhibitor. The gels were prepared from walleye pollack salted-surimi mixed with KBrO3 through setting at 30 degrees C (suwari gel) for 2 h prior to heating at 80 degrees C for 20 min (kamaboko gel) in the presence or absence of TGase inhibitor. The gel strength of kamaboko gel increased through setting but KBrO3 almost did not promote the gel formation of kamaboko gels through setting comparing with control. KBrO3 increased the breaking strength and decreased elongation so that the gel became harder. Even in the presence of TGase inhibitor, where the increase in gel strength during setting was suppressed, KBrO3 showed the promotion of gel formation, although the gel strength is lower than the gel without TGase inhibitor. Almost, similar behaviors of protein polymerization by disulfide bonds and the oxidation of sulfhydryl groups to those in the absence of TGase inhibitor were observed. These results suggest that KBrO3 enhances the gel forming ability of walleye pollack surimi through the disulfide bonding of myosin heavy chain by oxidation during the setting. In conclusion, the oxidation of salted surimi sol during setting at 30 degrees C can contribute to the gel formation, but its contribution seems not to be cooperative with that of TGase.
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http://dx.doi.org/10.3923/pjbs.2010.1.8 | DOI Listing |
Food Chem
February 2025
State Key Laboratory of Food Science and Resources, School of Food Science and Technology, Jiangnan University, Wuxi 214122, China; Jiangsu Key Laboratory of Advanced Food Manufacturing Equipment & Technology, Jiangnan University, Wuxi, Jiangsu, PR China.
Analyst
April 2024
Department of Chemistry, National Taiwan University, Taipei 106, Taiwan.
J Am Chem Soc
March 2024
School of Chemistry, Chemical Engineering and Biotechnology, Nanyang Technological University, Singapore 637371, Singapore.
Peptidoglycan (PG), an essential exoskeletal polymer in bacteria, is a well-known antibiotic target. PG polymerization requires the action of bacterial transglycosylases (TGases), which couple the incoming glycosyl acceptor to the donor. Interfering with the TGase activity can interrupt the PG assembly.
View Article and Find Full Text PDFEJNMMI Radiopharm Chem
January 2024
Helmholtz-Zentrum Dresden-Rossendorf, Institute of Radiopharmaceutical Cancer Research, Bautzner Landstraße 400, 01328, Dresden, Germany.
Background: Transglutaminase 2 (TGase 2) is a multifunctional protein and has a prominent role in various (patho)physiological processes. In particular, its transamidase activity, which is rather latent under physiological conditions, gains importance in malignant cells. Thus, there is a great need of theranostic probes for targeting tumor-associated TGase 2, and targeted covalent inhibitors appear to be particularly attractive as vector molecules.
View Article and Find Full Text PDFBioorg Chem
February 2024
School of Life Sciences, Gwangju Institute of Science and Technology, 123 Cheomdangwagi-ro, Buk-gu, Gwangju 61005, Republic of Korea. Electronic address:
Overexpression of transglutaminase 2 (TGase 2; TG2) has been implicated in the progression of renal cell carcinoma (RCC) through the inactivation of p53 by forming a protein complex. Because most p53 in RCC has no mutations, apoptosis can be increased by inhibiting the binding between TG2 and p53 to increase the stability of p53. In the present study, a novel TG2 inhibitor was discovered by investigating the structure of 1H-benzo[d]imidazole-4,7-dione as a simpler chemotype based on the amino-1,4-benzoquinone moiety of streptonigrin, a previously reported inhibitor.
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