Pilasombut, Komkhae

Preferred name

Pilasombut, Komkhae

Alternative Name

Pilasombut, K.

Main Affiliation

School of Agricultural Technology

komkhae.pi@kmitl.ac.th

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Purification and amino acid sequence of a bacteriocins produced by Lactobacillus salivarius K7 isolated from chicken intestine
(2006-01-01)
Pilasombut, Komkhae
;
Sakpuaram, Thavajchai
;
Wajjwalku, Worawidh
;
Nitisinprasert, Sunee
;
Swetwiwathana, Adisorn
A bacteriocin-producing strain, Lactobacillus K7, was isolated from a chicken intestine. The inhibitory activity was determined by spot-on-lawn technique. Identification of the strain was performed by morphological, biochemical (API 50 CH kit) and molecular genetic (16S rDNA) basis. Bacteriocin purification processes were carried out by amberlite adsorption, cation exchange and reverse-phase high perform ance liquid chromatography. N-terminal amino acid sequences were performed by Edman degradation. Molecular mass was determined by electrospray-ionization (ESI) mass spectrometry (MS). Lactobacillus K7 showed inhibitory activity against Lactobacillus sakei subsp. sakei JCM 1157T, Leuconostoc mesenteroides subsp. mesenteroides JCM 6124T and Bacillus coagulons JCM 2257T. This strain was identified as Lb. salivarius. The antimicrobial substance was destroyed by proteolytic enzymes, indicating its proteinaceous structure designated as a bacteriocin type. The purification of bacteriocin by amberlite adsorption, cation exchange, and reverse-phase chromatography resulted in only one single active peak, which was designated FK22. Molecular weight of this fraction was 4331.70 Da. By amino acid sequence, this peptide was homology to Abp 118 beta produced by Lb. salivarius UCC118. In addition, Lb. salivarius UCC118 produced 2-peptide bacteriocin, which was Abp 118 alpha and beta. Based on the partial amino acid sequences of Abp 118 beta, specific primers were designed from nucleotide sequences according to data from GenBank. The result showed that the deduced peptide was high homology to 2-peptide bacteriocin, Abp 118 alpha and beta.
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In vitro characterization of bacteriocin produced by lactic acid bacteria isolated from Nem Chua, a traditional Vietnamese fermented pork
(2015-08-01)
Pilasombut, Komkhae
;
Rumjuankiat, Kittaporn
;
Ngamyeesoon, Nualphan
;
Duy, Le Nguyen Doan
The aim of this study was to screen and In vitro characterize the properties of bacteriocin produced by lactic acid bacteria isolated from Vietnamese fermented pork (Nem chua). One hundred and fifty LAB were isolated from ten samples of Nem chua and screened for bacteriocin-producing lactic acid bacteria. Antimicrobial activity of bacteriocin was carried out by spot on lawn method against both gram positive and gram negative bacteria. One isolate, assigned as KL-1, produced bacteriocin and showed inhibitory activity against Lactobacillus sakei, Leuconostoc mesenteroides and Enterococcus faecalis. To characterize the bacteriocin-producing strain, optimum temperature, incubation period for maximum bacteriocin production and identification of bacteriocin-producing strain were determined. It was found that the optimum cultivation temperature of the strain to produce the maximum bacteriocin activity (12,800 AU/mL) was obtained at 30°C. Meanwhile, bacteriocin production at 6,400 AU/mL was found when culturing the strain at 37°C and 42°C. The isolate KL-1 was identified as L. plantarum. Antimicrobial activity of cell-free supernatant was completely inhibited by proteolytic enzyme of trypsin, alpha-chymotrypsin and proteinase K. Bacteriocin activity was stable at high temperature up to 100°C for 10 min and at 4°C storage for 2 d. However, the longer heating at 100°C and 4°C storage, its activity was reduced.
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Purification and characterization of a novel plantaricin, KL-1Y, from Lactobacillus plantarum KL-1
(2015-06-13)
Rumjuankiat, Kittaporn
;
Perez, Rodney Horanda
;
Pilasombut, Komkhae
;
Keawsompong, Suttipun
;
Zendo, Takeshi
Three bacteriocins from Lactobacillus plantarum KL-1 were successfully purified using ammonium sulfate precipitation, cation-exchange chromatography and reverse-phase HPLC. The bacteriocin peptides KL-1X, -1Y and -1Z had molecular masses of 3053.82, 3498.16 and 3533.16 Da, respectively. All three peptides were stable at pH 2–12 and 25 °C and at high temperatures of 80 and 100 °C for 30 min and 121 °C for 15 min. However, they differed in their susceptibility to proteolytic enzymes and their inhibition spectra. KL-1Y showed broad inhibitory activities against Gram-positive and Gram-negative bacteria, including Salmonella enterica serovar Enteritidis DMST 17368, Pseudomonas aeruginosa ATCC 15442, P. aeruginosa ATCC 9027, Escherichia coli O157:H7 and E. coli ATCC 8739. KL-1X and -1Z inhibited only Gram-positive bacteria. KL-1X, KL-1Y and KL-1Z exhibited synergistic activity. The successful amino acid sequencing of KL-1Y had a hydrophobicity of approximately 30 % and no cysteine residues suggested its novelty, and it was designated “plantaricin KL-1Y”. Plantaricin KL-1Y exhibited bactericidal activity against Bacillus cereus JCM 2152T. Compared to nisin, KL-1Y displayed broad inhibitory activities of 200, 800, 1600, 800, 400 and 400 AU/mL against the growth of Bacillus coagulans JCM 2257T, B. cereus JCM 2152T, Listeria innocua ATCC 33090T, Staphylococcus aureus TISTR 118, E. coli O157:H7 and E. coli ATCC 8739, respectively, whereas nisin had similar activities against only B. coagulans JCM 2257T and B. cereus JCM 2152T. Therefore, the novel plantaricin KL-1Y is a promising antimicrobial substance for food safety uses in the future.
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Effect of extracted pectin from fruit wastes on growth of Pediococcus pentosaceus RSU-Nh1 and Lactobacillus plantarum RSU-SO2
(2020-01-01)
Showpanish, K.
;
Sonhom, N.
;
Pilasombut, K.
;
Woraprayote, W.
;
Prachom, N.
Two strains of lactic acid bacteria identified as Pediococcus pentosaceus RSU-Nh1 and Lactobacillus plantarum RSU-SO2 were isolated from Thai fermented pork sausage (Nham) and fermented spring onion (Ton-Hom-Dong) respectively. The culture supernatant (CFS) of both strains exhibited antimicrobial activity against both Gram-positive and Gramnegative pathogenic bacteria. After being treated with alpha-chymotrypsin and trypsin, the antimicrobial activity of their CFS was eliminated, which suggests that the antimicrobial compound produced was antimicrobial peptide or bacteriocin. Pectin extracted from different fruit peels was supplemented in the bacterial growth medium to investigate the effect of pectin on the growth and antimicrobial production of Ped. pentosaceus RSU-Nh1 and Lb. plantarum RSU-SO2. Pectin was extracted from pomelo, durian, passion fruit and salacca fruit peels with a pectin yield of 5.02 to 26.44%, degree of esterification of 80.84 to 86.68%, and galacturonic acid content of 52.36 to 64.23%. Supplementation with pomelo and passion fruit pectin exhibited the highest improvement of bacterial growth and antimicrobial production of Ped. pentosaceus RSU-Nh1 and Lb. plantarum RSU-SO2. These findings suggested the potential application of these pectin extracts as prebiotics to promote the growth and antimicrobial production of lactic acid bacteria.

Pilasombut, Komkhae

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