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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   Pages 1 - 7 ( 7 )

Abstract:


Background: Plantaricin IIA-1A5 is a bacteriocin produced by Lactobacillus plantarum IIA-1A5, a locally isolat-ed probiotic from Indonesia. Plantaricin IIA-1A5 exhibits antibacterial activity against wide spectrum of pathogenic bacte-ria, 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 param-eters.

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 ion-exchange 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, thermo-dynamic parameters

Affiliation:

Department of Animal Production and Technology, Faculty of Animal Science, Bogor Agricultural University, Bogor,, Department of Animal Production and Technology, Faculty of Animal Science, Bogor Agricultural University, Bogor,, The International Center for Biotechnology, Osaka University, Osaka,, Department of Animal Production and Technology, Faculty of Animal Science, Bogor Agricultural University, Bogor



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