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Bacteriocins from lactic acid bacteria and their applications in meat and meat products
(2016-10-01)
Woraprayote, Weerapong
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Malila, Yuwares
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Sorapukdee, Supaluk
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Swetwiwathana, Adisorn
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Benjakul, Soottawat
Meat and meat products have always been an important part of human diet, and contain valuable nutrients for growth and health. Nevertheless, they are perishable and susceptible to microbial contamination, leading to an increased health risk for consumers as well as to the economic loss in meat industry. The utilization of bacteriocins produced by lactic acid bacteria (LAB) as a natural preservative has received a considerable attention. Inoculation of bacteriocin-producing LAB cell as starter or protective cultures is suitable for fermented meats, whilst the direct addition of bacteriocin as food additive is more preferable when live cells of LAB could not produce bacteriocin in the real meat system. The incorporation of bacteriocins in packaging is another way to improve meat safety to avoid direct addition of bacteriocin to meat. Utilization of bacteriocins can effectively contribute to food safety, especially when integrated into hurdle concepts. In this review, LAB bacteriocins and their applications in meat and meat products are revisited. The molecular structure and characteristics of bacteriocins recently discovered, as well as exemplary properties are also discussed.
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Potential of bacteriocin-producing lactic acid bacteria for safety improvements of traditional Thai fermented meat and human health
(2015-11-01)
Swetwiwathana, Adisorn
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Visessanguan, Wonnop
Lactic acid bacteria (LAB) are very important in converting of agricultural products into safe, delicious and shelf stable foods for human consumption. The preservative activity of LAB in foods is mainly attributed to the production of anti-microbial metabolites such as organic acids and bacteriocins which enables them to grow and control the growth of pathogens and spoilage microorganisms. Besides ensuring safety, bacteriocin-producing LAB with their probiotic potentials could also be emerging as a means to develop functional meat products with desirable health benefits. Nevertheless, to be qualified as a candidate probiotic culture, other prerequisite probiotic properties of bacteriocin-producing LAB have to be assessed according to regulatory guidelines for probiotics. Nham is an indigenous fermented sausage of Thailand that has gained popularity and acceptance among Thais. Since Nham is made from raw meat and is usually consumed without cooking, risks due to undesirable microorganisms such as Salmonella spp., Staphylococcus aureus, and Listeria monocytogenes, are frequently observed. With an ultimate goal to produce safer and healthier product, our research attempts on the development of a variety of new Nham products are discussed.
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Lactic acid bacterial population dynamics during fermentation and storage of Thai fermented sausage according to restriction fragment length polymorphism analysis
(2014-09-01)
Wanangkarn, Amornrat
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Liu, Deng Cheng
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Swetwiwathana, Adisorn
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Jindaprasert, Aphacha
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Phraephaisarn, Chirapiphat
This study applied restriction fragment length polymorphism (RFLP) analysis to identify the lactic acid bacteria (LAB) isolated from "mum" Thai fermented sausages during fermentation and storage. A total of 630 lactic acid bacteria were isolated from the sausages prepared using 2 methods. In Method 1, after stuffing, the sausages were stored at 30. °C for 14. days. In Method 2, after stuffing and storage at 30. °C for 3. days, the sausages were vacuum-packed and stored at 4. °C until Day 28. The sausages were sampled on Days 0, 3, 14, and 28 for analyses. The 16S rDNA was amplified and digested using restriction enzymes. Of the restriction enzymes evaluated, Dde I displayed the highest discrimination capacity. The LAB were classified and 7 species were identified For Methods 1 and 2, during fermentation, the Lactobacillus sakei and Lactobacillus plantarum species were dominant. For Method 2, the proportion of Leuconostoc mesenteroides markedly increased during storage, until L. sakei and Ln. mesenteroides represented the dominant species. The identification of LAB in the sausage samples could facilitate the selection of appropriate microorganisms for candidate starter cultures for future controlled mum production. © 2014 Elsevier B.V.
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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
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Sakpuaram, Thavajchai
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Wajjwalku, Worawidh
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Nitisinprasert, Sunee
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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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