Acta Alimentaria
Volume/Issue:
Volume 49: Issue 4
An Acylase from Shewanella Putrefaciens Presents a Vibrio Parahaemolyticus Acylhomoserine Lactone-Degrading Activity and Exhibits Temperature-, Ph- and Metal-Dependences
Authors:
Z. Fang College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524048, China

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D. Sun College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524048, China

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J. Gao College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524048, China

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M. Guo College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524048, China

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L. Sun College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524048, China

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Y. Wang College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524048, China

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Y. Lıu College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524048, China

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R. Wang College of Food Science and Engineering, Lingnan Normal University, Zhanjiang, 524048, China

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Q. Deng College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524048, China

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D. Xu College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524048, China

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R. Gooneratne Department of Wine, Food and Molecular Biosciences, Lincoln University, Lincoln, Canterbury, 7647, New Zealand

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Pages:
375–381
Online Publication Date:
07 Nov 2020
Publication Date:
07 Nov 2020
Article Category:
Research Article
DOI:
https://doi.org/10.1556/066.2020.49.4.2
Keywords:
acylase; AHL-degrading enzyme; acylhomoserine lactone; Shewanella putrefaciens; Vibrio parahaemolyticus
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Shewanella putrefaciens supernatant was found to increase the virulence factors of Vibrio parahaemolyticus by efficiently degrading its acylhomoserine lactone (AHL). To further reveal the regulation mechanism and its key degrading enzyme, a potential AHL-degrading enzyme acylase (Aac) from S. putrefaciens was cloned, and the influences of temperature, pH, protein modifiers, and metals on Aac were tested. Aac was significantly influenced by temperature and pH, and exhibited the highest AHL-degrading activity at temperatures of 37 °C and pH of 8. Mg2+ and Fe2+ can further increase the AHL-degrading activity. 10 mM EDTA inhibited its activity possibly by chelating the co-factors (metals) required for Aac activity. Tryptophan and arginine were identified as key components for Aac activity that are critical to its AHL-degrading activity. This study provides useful information on Aac and for V. parahaemolyticus control.

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Cover Acta Alimentaria
Acta Alimentaria
Print ISSN:
0139-3006
Online ISSN:
1588-2535

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

 

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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.
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ISSN 0139-3006 (Print)
ISSN 1588-2535 (Online)

 

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