By Fernanda Mozzi PhD, Rául R. Raya, Graciela M. Vignolo PhD
This title represents a large overview of present study on LAB and their novel purposes with contributions from a few famous major scientists. The publication contains a wide selection of subject matters together with either conventional and novel constructing fields, and gives unheard of, complete details on new advances of genomics, proteomics, metabolism and biodiversity of LAB. Chapters comprise cutting-edge discussions of particular LAB purposes akin to their use as probiotics, reside vaccines and starter cultures in previous and new fermented items. the security of those microorganisms and their interactions with diversified ecosystems ordinary biota also are coated in addition to the hot purposes of recognized (bacteriocins) and novel (vitamins, low-calorie sugars, etc.) metabolites produced via LAB.This e-book is a vital reference for proven researchers and scientists, doctoral and post-doctoral scholars, collage professors and teachers, and nutrition technologists engaged on meals microbiology, body structure and biotechnology of lactic acid micro organism.
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Additional info for Biotechnology of Lactic Acid Bacteria: Novel Applications
1998), and the CL-coding genes have been cloned from this strain (Bekal et al. 1998), from a plasmid belonging to a Weissella paramesenteroides strain (Martín et al. 1999, 2000), and from the chromosome of L. diacetylactis CRL264 (Martín et al. 2004). The second step of citrate metabolism, catalyzed by oxaloacetate decarboxylase (OAD), is the decarboxylation of oxaloacetate, generating pyruvate and CO2. Analysis of the genomes of various LAB indicate that a homolog of the Klebsiella pneumoniae OAD, the best characterized bacterial enzyme of this type, is only present in Strep.
Thermophilus. This finding agrees well with the experiments of Helinck et al. (2004), who showed these enzyme activities in Strep. thermophilus strains. Caution is required, however, since the best homologs of KaDH in many LAB are annotated as either pyruvate or acetoin dehydrogenase complex, and it is not clear whether these complexes have overlapping substrate specificity (Liu et al. 2008). Keto acids can also be reduced to hydroxy acids by hydroxy acid dehydrogenase (HADH). Two stereospecific enzymes, D-HADH and L-HADH, are distinguished, which belong to the larger D-LDH and L-LDH protein families, respectively.
Pentosaceus. 7. Biogenic Amines Pathways from Amino Acids Catabolism of some amino acids can produce biogenic amines (BAs), which can cause food poisoning. BAs are mainly formed by decarboxylation of the amino acids tyrosine, histidine, lysine, and ornithine (Fig. 3), from which tyramine, histamine, cadaverine, and putrescine, respectively, are produced. Tyrosine, histidine, and ornithine decarboxilase activities have been reported in LAB species and strains of Lactobacillus, Enterococcus, Oenococcus, Tetragenococcus, and Carnobacterium.