Authors:
T.D.L. Vo Department of Food Technology, Faculty of Chemical Engineering, Ho Chi Minh City University of Technology, 268 Ly Thuong Kiet Street, 72506, Ho Chi Minh City, Vietnam
Vietnam National University Ho Chi Minh City, 71308, Ho Chi Minh City, Vietnam

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V.K. Nguyen Department of Food Technology, Faculty of Chemical Engineering, Ho Chi Minh City University of Technology, 268 Ly Thuong Kiet Street, 72506, Ho Chi Minh City, Vietnam
Vietnam National University Ho Chi Minh City, 71308, Ho Chi Minh City, Vietnam

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T.T.P. Nguyen Department of Food Technology, Faculty of Chemical Engineering, Ho Chi Minh City University of Technology, 268 Ly Thuong Kiet Street, 72506, Ho Chi Minh City, Vietnam
Vietnam National University Ho Chi Minh City, 71308, Ho Chi Minh City, Vietnam

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B.C. Vo Department of Food Technology, Faculty of Chemical Engineering, Ho Chi Minh City University of Technology, 268 Ly Thuong Kiet Street, 72506, Ho Chi Minh City, Vietnam
Vietnam National University Ho Chi Minh City, 71308, Ho Chi Minh City, Vietnam

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T.T.T. Nguyen Pham Ngoc Thach Hospital, 120 Hong Bang Street, 72713, Ho Chi Minh City, Vietnam

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Abstract

This study aims to examine the effect of hydrolysis degree (DH) on both antioxidant activity and functional properties of Acetes japonicus proteolysate (AP). Consequently, the AP showed the highest 2,2-diphenyl-1-picrylhydrazyl (DPPH) scavenging activity (SA) and ferric reducing antioxidant power (FRAP) at DH of 66.7%. Whereas, 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) cation radical (ABTS•+) SA and superoxide anion radical (O2 •–) SA of the AP peaked at DH of 75.8%. In addition, its strongest Fe2+-chelating rate was found at DH of 72.1%. In the pH range from 3 to 8, the AP showed solubility over 55% even after heat treating, foaming capacity (FC) of 5.7–80.0%, foaming stability (FS) of 2.9–77.0%, emulsifying-activity index (EAI) of 16.1–56.3 m2 g−1, and emulsifying stability index (ESI) of 12.4–156.7 min. The highest water-holding capacity (WHC) and oil-holding capacity (OHC) of the AP were observed at DH of 66.7% and 50.6%, respectively. This study enhanced value of the Acetes by producing antioxidant AP possessing functionalities.

  • Charoenphun, N. , Cheirsilp, B. , Sirinupong, N. , and Youravong, W. (2013). Calcium-binding peptides derived from tilapia (Oreochromis niloticus) protein hydrolysate. European Food Research and Technology, 236(1): 5763.

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  • Halim, N.R.A. , Yusof, H.M. , and Sarbon, N.M. (2016). Functional and bioactive properties of fish protein hydolysates and peptides: a comprehensive review. Trends in Food Science & Technology, 51: 2433.

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  • Intarasirisawat, R. , Benjakul, S. , Visessanguan, W. , and Wu, J. (2012). Antioxidative and functional properties of protein hydrolysate from defatted skipjack (Katsuwonous pelamis) roe. Food Chemistry, 135(4): 30393048.

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  • Li, X. , Luo, Y. , Shen, H. , and You, J. (2012). Antioxidant activities and functional properties of grass carp (Ctenopharyngodon idellus) protein hydrolysates. Journal of the Science of Food and Agriculture, 92(2): 292298.

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  • Li, X. , Shen, S. , Deng, J. , Li, T. , and Ding, C. (2014). Antioxidant activities and functional properties of tea seed protein hydrolysates (Camellia oleifera Abel.) influenced by the degree of enzymatic hydrolysis. Food Science and Biotechnology, 23(6): 20752082.

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  • Noman, A. , Xu, Y. , AL-Bukhaiti, W.Q. , Abed, S.M. , Ali, A.H. , Ramadhan, A.H. , and Xia, W. (2018). Influence of enzymatic hydrolysis conditions on the degree of hydrolysis and functional properties of protein hydrolysate obtained from Chinese sturgeon (Acipenser sinensis) by using papain enzyme. Process Biochemistry, 67: 1928.

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  • Putra, S.N.K.M. , Ishak, N.H. , and Sarbon, N.M. (2018). Preparation and characterization of physicochemical properties of golden apple snail (Pomacea canaliculata) protein hydrolysate as affected by different proteases. Biocatalysis and Agricultural Biotechnology, 13: 123128.

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  • Santos, S.D.A.D. , Martins, V.G. , Salas-Mellado, M. , and Prentice, C. (2011). Evaluation of functional properties in protein hydrolysates from bluewing searobin (Prionotus punctatus) obtained with different microbial enzymes. Food and Bioprocess Technology, 4(8): 13991406.

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  • Siddik, M.A.B. , Howieson, J. , Fotedar, R. , and Partridge, G.J. (2021). Enzymatic fish protein hydrolysates in finfish aquaculture: a review. Reviews in Aquaculture, 13(1): 406430.

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  • Sila, A. and Bougatef, A. (2016). Antioxidant peptides from marine by-products: Isolation, identification and application in food systems. A review. Journal of Functional Foods, 21: 1026.

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  • Vo, T.D.L. , Pham, K.T. , Bui, N.H.Y. , Luong, N.N.Y. , Nguyen, N.T. , Mai, C T. , and Nguyen, A.H. (2021a). Identification of a new antioxidant peptide from protein hydrolysate of Acetes japonicus. Proceeding of the 5th International Conference on Chemical Engineering, Food and Biotechnology - ICCFB2021: pp. 5866.

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  • Vo, T.D.L. , Pham, K.T. , and Doan, K.T. (2021b). Identification of copper-binding peptides and investigation of functional properties of Acetes japonicus proteolysate. Waste and Biomass Valorization, 12: 15651579.

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  • Vo, T.D.L. , Pham, K.T. , Le, L.T. , and Nguyen, T.T.H. (2018). Identification of a new calcium‐binding peptide from enzymatic proteolysate of Acetes japonicus. Journal of Food Processing and Preservation, 42(12): e13837.

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  • Vo, T.D.L. , Pham, K.T. , Le, V.M.V. , Lam, H.H. , Huynh, O.N. , and Vo, B.C. (2020). Evaluation of iron-binding capacity, amino acid composition, functional properties of Acetes japonicus proteolysate and identification of iron-binding peptides. Process Biochemistry, 91: 374386.

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  • You, L. , Zhao, M. , Cui, C. , Zhao, H. , and Yang, B. (2009). Effect of degree of hydrolysis on the antioxidant activity of loach (Misgurnus anguillicaudatus) protein hydrolysates. Innovative Food Science and Emerging Technologies, 10: 235240.

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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)
  • 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)
  • H. He (Henan Institute of Science and Technology, Xinxiang, China)
  • 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
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Acta Alimentaria
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