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

被引:1
|
作者
Arifin, Muhamad [1 ]
Budiman, Cahyo [1 ]
Fujiyama, Kazuhito [2 ]
Arief, Irma Isnafia [1 ]
机构
[1] Bogor Agr Univ, Fac Anim Sci, Dept Anim Prod & Technol, Bogor, Indonesia
[2] Osaka Univ, Int Ctr Biotechnol, Osaka, Japan
来源
PROTEIN AND PEPTIDE LETTERS | 2021年 / 28卷 / 06期
关键词
Bacteriocin; biopreservatives; kinetic parameters; Lactobacillus plantarum IIA-1A5; plantaricin IIA-1A5; thermo-dynamic parameters; THERMAL INACTIVATION; EXTRACT;
D O I
10.2174/0929866527999201123213841
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 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 degrees 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 degrees 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 degrees 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.
引用
收藏
页码:680 / 686
页数:7
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