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Protein & Peptide Letters

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ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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Research Article

Kinetic and Thermodynamic Study of Plantaricin IIA-1A5, a Bacteriocin Produced by Indonesian Probiotic Lactobacillus plantarum IIA-1A5

Author(s): Muhamad Arifin*, Cahyo Budiman, Kazuhito Fujiyama and Irma Isnafia Arief

Volume 28, Issue 6, 2021

Published on: 23 November, 2020

Page: [680 - 686] Pages: 7

DOI: 10.2174/0929866527999201123213841

Price: $65

Abstract

Background: Plantaricin IIA-1A5 is a bacteriocin produced by Lactobacillus plantarum IIA-1A5, a locally isolated probiotic from Indonesia. Plantaricin IIA-1A5 exhibits antibacterial activity against wide spectrum of pathogenic bacteria, thus promising to be applied in various food products. Nevertheless, thermal stability of this bacteriocin remains to be fully investigated.

Objective: This study aims to determine thermal stability of plantaricin IIA-1A5 through kinetic and thermodynamic parameters.

Method: To address, plantaricin IIA-1A5 was purified from Lactobacillus plantarum IIA-1A5, which was growth under whey media, using ammonium sulfate precipitation followed by ionexchange chromatography. Purified plantaricin IIA-IA5 was then subjected to analysis of its bacteriocin activity. The thermal inactivation of bacteriocin from L. plantarum IIA-1A5 was calculated by incubating the bacteriocin at different temperatures ranging from 60-80 °C for 30 to 90 min, which was then used to calculate its kinetic and thermodynamic parameters.

Results: The result showed the inactivation rates (k-value) were ranging from 0.008 to 0.013 min-1. Heat resistance of plantaricin IIA-1A5 (D-value) at constant heating temperature of 60, 65, 70, 75, and 80 °C were 311.6, 305.9, 294.5, 198.9, and 180.2 min, which indicated a faster inactivation at higher temperatures. D-value sensitivity for temperature changes (z-value) was calculated to be 75.76 °C. Further, thermodynamic analysis suggested that plantaricin IIA-1A5 is thermostable, with activation energy (Ea) of 29.02 kJ mol-1.

Conclusion: This result showed that plantaricin IIA-1A5 is considerably more heat-stable than plantaricin members and promises to be applied in food industries where heat treatments are applied. Furthermore, a possible mechanism by which plantaricin IIA-1A5 maintains its stability was also discussed by referring to its thermodynamic parameters.

Keywords: Bacteriocin, biopreservatives, kinetic parameters, Lactobacillus plantarum IIA-1A5, plantaricin IIA-1A5, thermodynamic parameters.

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[1]
WHO. WHO estimates of the global burden of foodborne diseases: foodborne disease burden epidemiology reference group 2007-2015; WHO Library Cataloguing-in-Publication Data, 2015.
[2]
Pal, S. Incidence of foodborne illness. US Pharm., 2017, 42(12), 14.https://www.uspharmacist.com
[3]
Cotter, P.D.; Ross, R.P.; Hill, C. Bacteriocins - a viable alternative to antibiotics? Nat. Rev. Microbiol., 2013, 11(2), 95-105.
[http://dx.doi.org/10.1038/nrmicro2937] [PMID: 23268227]
[4]
Cleveland, J.; Montville, T.J.; Nes, I.F.; Chikindas, M.L. Bacteriocins: safe, natural antimicrobials for food preservation. Int. J. Food Microbiol., 2001, 71(1), 1-20.
[http://dx.doi.org/10.1016/S0168-1605(01)00560-8] [PMID: 11764886]
[5]
Espachs-Barroso, A.; Loey, A.V.; Hendrickx, M.; Martín-Belloso, O. Inactivation of plant pectin methylesterase by thermal or high intensity pulsed electric field treatments. Innov. Food Sci. Emerg., 2006, 7, 40-48.
[http://dx.doi.org/10.1016/j.ifset.2005.07.002]
[6]
Hata, T.; Tanaka, R.; Ohmomo, S. Isolation and characterization of plantaricin ASM1: a new bacteriocin produced by Lactobacillus plantarum A-1. Int. J. Food Microbiol., 2010, 137(1), 94-99.
[http://dx.doi.org/10.1016/j.ijfoodmicro.2009.10.021] [PMID: 19939484]
[7]
Sant’anna, V.; Utpott, M.; Cladera-Olivera, F.; Brandelli, A. Kinetic modeling of the thermal inactivation of bacteriocin-like inhibitory substance p34. J. Agric. Food Chem., 2010, 58(5), 3147-3152.
[http://dx.doi.org/10.1021/jf903626w] [PMID: 20131794]
[8]
Arief, I.I. Jakaria; Suryati, T.; Wulandari, Z.; Andreas, E. Isolation and characterization of plantaricin produced by Lactobacillus plantarum Strain (IIA/1A5,IIA/1B1, IIA/2B2). Trop Anim Sci., 2013, 36(2), 91-100.
[http://dx.doi.org/10.5398/medpet.2013.36.2.91]
[9]
Sulaiman, N.B.; Irma, I.A.; Cahyo, B. Characteristic of lamb sausages fermented by indonesian meat-derived probiotic, Lactobacillus plantarum IIA-2C12 and Lactobacillus acidophilus IIA-2B4. Trop Anim Sci., 2016, 39(2), 104-111.
[http://dx.doi.org/10.5398/medpet.2016.39.2.104]
[10]
Kia, K.; Irma, I.A.; Cece, S.; Cahyo, B. Plantaricin IIA-1A5 from L. plantarum IIA-1A5 retards pathogenic bacteria in beef meatball stored at room temperature. Am. J. Food Technol., 2016, 11(1-2), 37-43.
[11]
Fatmarani, R.; Irma, I.A.; Cahyo, B. Purification of bacteriocin from Lactobacillus plantarum IIA-1A5 grown in various whey cheese media under freeze dried condition. Trop Anim Sci., 2018, 41(1), 53-59.
[http://dx.doi.org/10.5398/tasj.2018.41.1.53]
[12]
Dhiman, A.; Nanda, A.; Ahmad, S.; Narasimhan, B. In vitro antimicrobial activity of methanolic leaf extract of Psidium guajava L. J. Pharm. Bioallied Sci., 2011, 3(2), 226-229.
[http://dx.doi.org/10.4103/0975-7406.80776] [PMID: 21687350]
[13]
Thirumurugan, A.; Ramachandran, S.; Sivamani, S. Bacteriocin produced from Lactobacillus plantarum ATM11: kinetic and thermodynamic studies. Int. J. Food Eng., 2016, 12(5), 501-505.
[http://dx.doi.org/10.1515/ijfe-2015-0376]
[14]
Arief, I.I.; Budiman, C.; Jenie, B.S.; Andreas, E.; Yuneni, A. Plantaricin IIA-1A5 from Lactobacillus plantarum IIA-1A5 displays bactericidal activity against Staphylococcus aureus. Benef. Microbes, 2015, 6(4), 603-613.
[http://dx.doi.org/10.3920/BM2014.0064] [PMID: 25809213]
[15]
Gouzi, H.; Depagne, C.; Coradin, T. Kinetics and thermodynamics of the thermal inactivation of polyphenol oxidase in an aqueous extract from Agaricus bisporus. J. Agric. Food Chem., 2012, 60(1), 500-506.
[http://dx.doi.org/10.1021/jf204104g] [PMID: 22148350]
[16]
Fields, P.A.; Dong, Y.; Meng, X.; Somero, G.N. Adaptations of protein structure and function to temperature: there is more than one way to ‘skin a cat’. J. Exp. Biol., 2015, 218(Pt 12), 1801-1811.
[http://dx.doi.org/10.1242/jeb.114298] [PMID: 26085658]
[17]
Sant’Anna, V.; Florencia, C.O.; Adriano, B. Kinetic and thermodynamic study of thermal inactivation of the antimicrobial peptide P34 in milk. J. Food Chem., 2012, 130(1), 84-89.
[http://dx.doi.org/10.1016/j.foodchem.2011.07.001]
[18]
Deylami, M.Z.R.A.; Chin, P.T.; Jamilah, B.; Llasekan, O. Thermodynamics and kinetics of thermal inactivation of peroxidase from mangosteen (Garcinia mangostana L.) Pericarp. J. Eng. Sci. Technol., 2014, 9(3), 374-383.
[19]
Akazawa-Ogawa, Y.; Uegaki, K.; Hagihara, Y. The role of intra-domain disulfide bonds in heat-induced irreversible denaturation of camelid single domain VHH antibodies. J. Biochem., 2016, 159(1), 111-121.
[http://dx.doi.org/10.1093/jb/mvv082] [PMID: 26289739]
[20]
Lappe, R.; Cladera-Olivera, F.; Dominguez, A.P.M.; Brandelli, A. Kinetics and thermodynamics of thermal inactivation of the antimicrobial peptide cerein 8A. J. Food Eng., 2009, 91(2), 223-227.
[http://dx.doi.org/10.1016/j.jfoodeng.2008.08.025]
[21]
Dagan, S.; Hagai, T.; Gavrilov, Y.; Kapon, R.; Levy, Y.; Reich, Z. Stabilization of a protein conferred by an increase in folded state entropy. Proc. Natl. Acad. Sci. USA, 2013, 110(26), 10628-10633.
[http://dx.doi.org/10.1073/pnas.1302284110] [PMID: 23754389]

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