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  • a College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, 524048, China
  • | b College of Food Science and Engineering, Lingnan Normal University, Zhanjiang, 524048, China
  • | c Department of Wine, Food and Molecular Biosciences, Lincoln University, Lincoln, Canterbury, 7647, New Zealand
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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.

  • Croyder, M.W., Maıtı, M.K., Banovıc, L. & Makaroff, CA. (1997): Glyoxalase II from A. thaliana requires Zn(II) for catalytic activity. FEBS Lett., 418(3), 351354.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Dıkler, S., Kelly, J.W. & Russell, D.H. (2015): Improving mass spectrometric sequencing of arginine-containing peptides by derivatization with acetylacetone. J. Mass Spectrom., 32(12), 13371349.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Fang, Z., Kuanu, X., Zhanu, Y., Shı, P. & Huang, Z. (2015): A novel HAC1-based dual-luciferase reporter vector for detecting endoplasmic reticulum stress and unfolded protein response in yeast Saccharomyces cerevisiae. Plasmid, 79, 4853.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Fang, Z., Sun, D., , C., Sun, L., Wang, Y., Guo, M., & Lıu, Y. (2018): Regulatory effects of Shewanella putrefaciens isolated from shrimp Penaeus orientalis on the virulence factors of Vibrio parahaemolyticus and evaluation of the role of quorum sensing in virulence factors regulation. FEMS Microbiol. Ecol., 94(7), fiy097.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Ghaneımotlauh, R., Mohammadıan, T., Gharıbı, D., Menanteauledouble, S., Mahmoudı, E., & Elmatboulı, M. (2019): Quorum quenching properties and probiotic potentials of intestinal associated bacteria in Asian sea bass Lates calcarifer. Mar. Drugs, 18(1), 23.

    • Search Google Scholar
    • Export Citation
  • Gode, C.J. (2011): Vibrio parahaemolyticus responds to growth on a surface by initiating a program of gene control that is regulated by calcium, iron, and quorum sensing. (PhD Thesis), University of Iowa, Iowa, US. 208 pages.

    • Search Google Scholar
    • Export Citation
  • Gode-Potratz, C.J., Chodur, D.M. & Mccarter, L.L. (2010): Calcium and iron regulate swarming and type III secretion in Vibrio parahaemolyticus. J. Bacteriol., 192(22), 6025.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Gutıerrez West, C.K., Kleın, S.L. & Lovell, C.R. (2013): High frequency of virulence factor genes tdh, trh, and tlh in Vibrio parahaemolyticus strains isolated from a pristine estuary. Appl. Environ. Microb., 79(7), 22472252.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Hammer, B.K. & Bassler, B.L. (2003): Quorum sensing controls biofilm formation in Vibrio cholerae. Mol. Microbiol., 50(1), 101104.

  • Iunatova, Z., Wıschneyskı, F., Notbohm, H. & Kasche, V. (2005): Pro-sequence and Ca2+-binding: Implications for folding and maturation of ntn-hydrolase penicillin amidase from E. coli. J. Mol. Biol., 348(4), 9991014.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Kanu, C. & So, J. (2016): Antibiotic and heavy metal resistance in Shewanella putrefaciens strains isolated from shellfishes collected from West Sea, Korea. Mar. Pollut. Bull., 112(1), 111116.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Kım, J.K., Yanu, I.S., Shın, H.J., Cho, K.J., Ryu, E.K., Kım, S.H., & Kım, K. H. (2006): Insight into autoproteolytic activation from the structure of cephalosporin acylase: A protein with two proteolytic chemistries. P. Natl. Acad. Sci. USA., 103(6), 17321737.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Kım, Y., Yoon, K.-H., Khanu, Y., Turley, S. & Hol, W.G. (2000): The 2.0 A crystal structure of cephalosporin acylase. Structure, 8(10), 10591068.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Kımes, N.E., Grım, C.J., Johnson, W.R., Hasan, N.A., Tall, B.D., Kothary, M.H., & Morrıs, P.J. (2012): Temperature regulation of virulence factors in the pathogen Vibrio coralliilyticus. ISME J, 6(4), 835846.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Leadbetter, J.R. & Greenberu, E.P. (2000): Metabolism of acyl-homoserine lactone quorum-sensing signals by Variovorax paradoxus. J. Bacteriol., 182(24), 69216926.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Lee, Y.S., Kım, H.W., Kanu, B.L. & Park, S.S. (2000): Involvement of arginine and tryptophan residues in catalytic activity of glutaryl 7-aminocephalosporanic acid acylase from Pseudomonas sp. strain GK16. Biochim. Biophys. Acta, 1523(1), 123127.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Lın, Y., Xu, J., Hu, J., Wang, L., Onu, S.L., Leadbetter, J.R., Zhanu, L.H. (2003): Acyl-homoserine lactone acylase from Ralstonia strain XJ12B represents a novel and potent class of quorum-quenching enzymes. Mol. Microbiol., 47(3), 849860.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Melıno, S., Capo, C., Drauanı, B., Aceto, A. & Petruzzellı, R. (1998): A zinc-binding motif conserved in glyoxalase II, beta-lactamase and arylsulfatases. Trends Biochem. Sci, 23(10), 381382.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Mochızukı, K. (2001): Purification and characterization of a lactonase from Burkholderia sp. R-711, that hydrolyzes (R)-5-oxo-2-tetrahydrofurancar-boxylic acid. Arch. Microbiol., 175(6), 430434.

    • Search Google Scholar
    • Export Citation
  • Moruan, W.T. & Mullereberhard, U. (1976): Chemical modification of histidine residues of rabbit hemopexin. Arch. Biochem. Biophys., 176(2), 431441.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Morohoshı, T., Nakazaya, S., Ebata, A., Kato, N. & Ikeda, T. (2008): Identification and characterization of N-acylhomoserine lactone-acylase from the fish intestinal Shewanella sp. strain MIB015. Biosci., Biotech., Bioch., 72(7), 18871893.

    • Search Google Scholar
    • Export Citation
  • Nakaı, T., Kanno, T., Cruz, E.R. & Muroua, K. (1987): The effects of iron compounds on the virulence of Vibrio anguillarum in Japanese eels and ayu. Fish Pathol., 22(4), 185189.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Shıh, P.C. & Huang, C.T. (2002): Effects of quorum-sensing deficiency on Pseudomonas aeruginosa biofilm formation and antibiotic resistance. J. Antimicrob. Chemoth., 49(2), 309314.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Steınberu, J.P. & Burd, E.M. (2015): 238-Other Gram-negative and Gram-variable bacilli.-in: Bennett, J.E., Dolın, R & Blaser, M.J. (Eds): Mandell, Douglas, and Bennett’s principles and practice of infectious diseases 8th. Saunders Elsevier, Philadelphia. pp. 26672683

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Tenu, L.R., Fan, H., Zhanu, Y.Q., , Y.U., Huang, Y.F. & Lıu, L.Y. (2006): Chemical modification and fluorescence spectrum of tryptophan residues in pullulanase. Chem. Res. Chinese U., 22(01), 6972.

    • Search Google Scholar
    • Export Citation
  • Tınh, N.T.N., Gunasekara, R.A.Y.S., Boon, N., Dıerckens, K., Sorueloos, P. & Bossıer, P. (2007): N-acyl homoserine lactone-degrading microbial enrichment cultures isolated from Penaeus vannamei shrimp gut and their probiotic properties in Brachionus plicatilis cultures. FEMS Microbiol. Ecol., 62(1), 4553.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Tsou, A.M. & Zhu, J. (2010): Quorum sensing negatively regulates hemolysin transcriptionally and posttranslationally in Vibrio cholerae. Infect. Immun., 78(1), 461467.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Wang, L.H., Wenu, L.X., Donu, Y.H. & Zhanu, L.H. (2004): Specificity and enzyme kinetics of the quorum-quenching N-acyl homoserine lactone lactonase (AHL-lactonase). J. Biol. Chem, 279(14), 1364513651.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Wrıuht, M.H., Mattheys, B., Arnold, M.S.J., Greene, A.C. & Cock, I.E. (2016): The prevention of fish spoilage by high antioxidant Australian culinary plants: Shewanella putrefaciens growth inhibition. Int. J. Food Sci. Tech., 51(3), 801813.

    • Crossref
    • Search Google Scholar
    • Export Citation
  • Zou, C., Duan, X. & Wu, J. (2016): Magnesium ions increase the activity of Bacillus deramificans pullulanase expressed by Brevibacillus choshinensis. Appl. Microbiol. Biot., 100(16), 71157123.

    • Crossref
    • Search Google Scholar
    • Export Citation

 

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Senior editors

Editor(s)-in-Chief: András Salgó

Co-ordinating Editor(s) Marianna Tóth-Markus

Co-editor(s): A. Halász

       Editorial Board

  • L. Abrankó (Szent István University, Gödöllő, Hungary)
  • D. Bánáti (University of Szeged, Szeged, Hungary)
  • J. Baranyi (Institute of Food Research, Norwich, UK)
  • I. Bata-Vidács (Agro-Environmental Research Institute, National Agricultural Research and Innovation Centre, Budapest, Hungary)
  • J. Beczner (Food Science Research Institute, National Agricultural Research and Innovation Centre, Budapest, Hungary)
  • F. Békés (FBFD PTY LTD, Sydney, NSW Australia)
  • Gy. Biró (National Institute for Food and Nutrition Science, Budapest, Hungary)
  • A. Blázovics (Semmelweis University, Budapest, Hungary)
  • F. Capozzi (University of Bologna, Bologna, Italy)
  • M. Carcea (Research Centre for Food and Nutrition, Council for Agricultural Research and Economics Rome, Italy)
  • Zs. Cserhalmi (Food Science Research Institute, National Agricultural Research and Innovation Centre, Budapest, Hungary)
  • M. Dalla Rosa (University of Bologna, Bologna, Italy)
  • I. Dalmadi (Szent István University, Budapest, Hungary)
  • K. Demnerova (University of Chemistry and Technology, Prague, Czech Republic)
  • M. Dobozi King (Texas A&M University, Texas, USA)
  • Muying Du (Southwest University in Chongqing, Chongqing, China)
  • S. N. El (Ege University, Izmir, Turkey)
  • S. B. Engelsen (University of Copenhagen, Copenhagen, Denmark)
  • E. Gelencsér (Food Science Research Institute, National Agricultural Research and Innovation Centre, Budapest, Hungary)
  • V. M. Gómez-López (Universidad Católica San Antonio de Murcia, Murcia, Spain)
  • J. Hardi (University of Osijek, Osijek, Croatia)
  • K. Héberger (Research Centre for Natural Sciences, ELKH, Budapest, Hungary)
  • N. Ilić (University of Novi Sad, Novi Sad, Serbia)
  • D. Knorr (Technische Universität Berlin, Berlin, Germany)
  • H. Köksel (Hacettepe University, Ankara, Turkey)
  • K. Liburdi (Tuscia University, Viterbo, Italy)
  • M. Lindhauer (Max Rubner Institute, Detmold, Germany)
  • M.-T. Liong (Universiti Sains Malaysia, Penang, Malaysia)
  • M. Manley (Stellenbosch University, Stellenbosch, South Africa)
  • M. Mézes (Szent István University, Gödöllő, Hungary)
  • Á. Németh (Budapest University of Technology and Economics, Budapest, Hungary)
  • P. Ng (Michigan State University,  Michigan, USA)
  • Q. D. Nguyen (Szent István University, Budapest, Hungary)
  • L. Nyström (ETH Zürich, Switzerland)
  • L. Perez (University of Cordoba, Cordoba, Spain)
  • V. Piironen (University of Helsinki, Finland)
  • A. Pino (University of Catania, Catania, Italy)
  • M. Rychtera (University of Chemistry and Technology, Prague, Czech Republic)
  • K. Scherf (Technical University, Munich, Germany)
  • R. Schönlechner (University of Natural Resources and Life Sciences, Vienna, Austria)
  • A. Sharma (Department of Atomic Energy, Delhi, India)
  • A. Szarka (Budapest University of Technology and Economics, Budapest, Hungary)
  • M. Szeitzné Szabó (National Food Chain Safety Office, Budapest, Hungary)
  • S. Tömösközi (Budapest University of Technology and Economics, Budapest, Hungary)
  • L. Varga (University of West Hungary, Mosonmagyaróvár, Hungary)
  • R. Venskutonis (Kaunas University of Technology, Kaunas, Lithuania)
  • B. 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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2020
 
Total Cites
768
WoS
Journal
Impact Factor
0,650
Rank by
Nutrition & Dietetics 79/89 (Q4)
Impact Factor
Food Science & Technology 130/144 (Q4)
Impact Factor
0,575
without
Journal Self Cites
5 Year
0,899
Impact Factor
Journal
0,17
Citation Indicator
 
Rank by Journal
Nutrition & Dietetics 88/103 (Q4)
Citation Indicator
Food Science & Technology 142/160 (Q4)
Citable
59
Items
Total
58
Articles
Total
1
Reviews
Scimago
28
H-index
Scimago
0,237
Journal Rank
Scimago
Food Science Q3
Quartile Score
 
Scopus
248/238=1,0
Scite Score
 
Scopus
Food Science 216/310 (Q3)
Scite Score Rank
 
Scopus
0,349
SNIP
 
Days from
100
sumbission
 
to acceptance
 
Days from
143
acceptance
 
to publication
 
Acceptance
16%
Rate
2019  
Total Cites
WoS
522
Impact Factor 0,458
Impact Factor
without
Journal Self Cites
0,433
5 Year
Impact Factor
0,503
Immediacy
Index
0,100
Citable
Items
60
Total
Articles
59
Total
Reviews
1
Cited
Half-Life
7,8
Citing
Half-Life
9,8
Eigenfactor
Score
0,00034
Article Influence
Score
0,077
% Articles
in
Citable Items
98,33
Normalized
Eigenfactor
0,04267
Average
IF
Percentile
7,429
Scimago
H-index
27
Scimago
Journal Rank
0,212
Scopus
Scite Score
220/247=0,9
Scopus
Scite Score Rank
Food Science 215/299 (Q3)
Scopus
SNIP
0,275
Acceptance
Rate
15%

 

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Acta Alimentaria
Language English
Size B5
Year of
Foundation
1972
Publication
Programme
2021 Volume 50
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
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
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Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 0139-3006 (Print)
ISSN 1588-2535 (Online)

 

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