Authors:
Y. Bai Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, P. R. China

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X. Li Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, P. R. China

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C. Ren Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, P. R. China

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X. Zheng Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, P. R. China

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C. Hou Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, P. R. China

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L. Chen Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, P. R. China

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D. Zhang Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, P. R. China

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Abstract

The activity and structural variation of glycogen phosphorylase (GP) at different phosphorylation levels during incubation at 4 °C were explored in this study. The GP was assigned into four treatments to obtain high/low phosphorylation levels, which were (1) treated with glycogen phosphorylase kinase (Phk) to obtain high phosphorylation level, (2) treated with protein kinase A to obtain high phosphorylation level, (3) treated with alkaline phosphatase to obtain low phosphorylation level, and (4) control. Compared with the control group, the content of α-helix and β-sheet increased and the secondary structure of GP changed from disorder to order after phosphorylation. The activity of GP was increased and its structure was more tightly in the Phk group than that in the control group. The phosphorylation at Ser277, Ser430, Ser809, Thr304, Tyr298, and Tyr525 resulted in tighter spatial structure. In conclusion, phosphorylation of GP enhanced its catalytic activity by making the secondary and spatial structure more orderly, which is of great significance for controlling meat quality by regulating glycolysis.

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Senior editors

Editor(s)-in-Chief: András Salgó, Budapest University of Technology and Economics, Budapest, Hungary

Co-ordinating Editor(s) Marianna Tóth-Markus, Budapest, Hungary

Co-editor(s): A. Halász, Budapest, Hungary

       Editorial Board

  • László Abrankó, Hungarian University of Agriculture and Life Sciences, Budapest, Hungary
  • Tamás Antal, University of Nyíregyháza, Nyíregyháza, Hungary
  • Diána Bánáti, University of Szeged, Szeged, Hungary
  • József Baranyi, Institute of Food Research, Norwich, UK
  • Ildikó Bata-Vidács, Eszterházy Károly Catholic University, Eger, Hungary
  • Ferenc Békés, FBFD PTY LTD, Sydney, NSW Australia
  • György Biró, Budapest, Hungary
  • Anna Blázovics, Semmelweis University, Budapest, Hungary
  • Francesco Capozzi, University of Bologna, Bologna, Italy
  • Marina Carcea, Research Centre for Food and Nutrition, Council for Agricultural Research and Economics Rome, Italy
  • Zsuzsanna Cserhalmi, Budapest, Hungary
  • Marco Dalla Rosa, University of Bologna, Bologna, Italy
  • István Dalmadi, Hungarian University of Agriculture and Life Sciences, Budapest, Hungary
  • Katarina Demnerova, University of Chemistry and Technology, Prague, Czech Republic
  • Mária Dobozi King, Texas A&M University, Texas, USA
  • Muying Du, Southwest University in Chongqing, Chongqing, China
  • Sedef Nehir El, Ege University, Izmir, Turkey
  • Søren Balling Engelsen, University of Copenhagen, Copenhagen, Denmark
  • Éva Gelencsér, Budapest, Hungary
  • Vicente Manuel Gómez-López, Universidad Católica San Antonio de Murcia, Murcia, Spain
  • Jovica Hardi, University of Osijek, Osijek, Croatia
  • Hongju He, Henan Institute of Science and Technology, Xinxiang, China
  • Károly Héberger, Research Centre for Natural Sciences, ELKH, Budapest, Hungary
  • Nebojsa Ilić, University of Novi Sad, Novi Sad, Serbia
  • Dietrich Knorr, Technische Universität Berlin, Berlin, Germany
  • Hamit Köksel, Hacettepe University, Ankara, Turkey
  • Katia Liburdi, Tuscia University, Viterbo, Italy
  • Meinolf Lindhauer, Max Rubner Institute, Detmold, Germany
  • Min-Tze Liong, Universiti Sains Malaysia, Penang, Malaysia
  • Marena Manley, Stellenbosch University, Stellenbosch, South Africa
  • Miklós Mézes, Hungarian University of Agriculture and Life Sciences, Gödöllő, Hungary
  • Áron Németh, Budapest University of Technology and Economics, Budapest, Hungary
  • Perry Ng, Michigan State University,  Michigan, USA
  • Quang Duc Nguyen, Hungarian University of Agriculture and Life Sciences, Budapest, Hungary
  • Laura Nyström, ETH Zürich, Switzerland
  • Lola Perez, University of Cordoba, Cordoba, Spain
  • Vieno Piironen, University of Helsinki, Finland
  • Alessandra Pino, University of Catania, Catania, Italy
  • Mojmir Rychtera, University of Chemistry and Technology, Prague, Czech Republic
  • Katharina Scherf, Technical University, Munich, Germany
  • Regine Schönlechner, University of Natural Resources and Life Sciences, Vienna, Austria
  • Arun Kumar Sharma, Department of Atomic Energy, Delhi, India
  • András Szarka, Budapest University of Technology and Economics, Budapest, Hungary
  • Mária Szeitzné Szabó, Budapest, Hungary
  • Sándor Tömösközi, Budapest University of Technology and Economics, Budapest, Hungary
  • László Varga, Széchenyi István University, Mosonmagyaróvár, Hungary
  • Rimantas Venskutonis, Kaunas University of Technology, Kaunas, Lithuania
  • Barbara Wróblewska, Institute of Animal Reproduction and Food Research, Polish Academy of Sciences Olsztyn, Poland

 

Acta Alimentaria
E-mail: Acta.Alimentaria@uni-mate.hu

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Acta Alimentaria
Language English
Size B5
Year of
Foundation
1972
Volumes
per Year
1
Issues
per Year
4
Founder Magyar Tudományos Akadémia    
Founder's
Address
H-1051 Budapest, Hungary, Széchenyi István tér 9.
Publisher Akadémiai Kiadó
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Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 0139-3006 (Print)
ISSN 1588-2535 (Online)

 

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