Biochemical Characterization of α-Galactosidase-Producing Thermophilic Bacillus coagulans KM-1

Nam, Ki-Ho; Jang, Mi-Soon; 박희연,; 코네바, 이레나

doi:10.5657/kfas.2014.0516

Cited by 5 publications

(3 citation statements)

References 16 publications

(5 reference statements)

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“…However, the electrophoretic mobility of this band (within the 130–180 KDa gel region) was identical to that identified as GH36 (Uniprot code: G2TQE8, Additional file 1 : Table S1) thus indicating that the enzymatic activity revealed by zymography, can be ascribed to the same protein. Besides our experimental evidences, the extracellular localization of the α-galactosidase has been previously described for another closely related B. coagulans strain [ 31 , 45 ] as well as for other soil microorganisms [ 46 ] and for Bacillus megaterium [ 47 ]. It is known that galactomannans are present in seeds of bean and, in general, RFOs (raffinose, stachyose, and verbascose) that contain α 1–6-linked galactose units, are particularly abundant in these legumes [ 9 ].…”

Section: Resultssupporting

confidence: 56%

Prebiotic properties of Bacillus coagulans MA-13: production of galactoside hydrolyzing enzymes and characterization of the transglycosylation properties of a GH42 β-galactosidase

et al. 2021

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Background The spore-forming lactic acid bacterium Bacillus coagulans MA-13 has been isolated from canned beans manufacturing and successfully employed for the sustainable production of lactic acid from lignocellulosic biomass. Among lactic acid bacteria, B. coagulans strains are generally recognized as safe (GRAS) for human consumption. Low-cost microbial production of industrially valuable products such as lactic acid and various enzymes devoted to the hydrolysis of oligosaccharides and lactose, is of great importance to the food industry. Specifically, α- and β-galactosidases are attractive for their ability to hydrolyze not-digestible galactosides present in the food matrix as well as in the human gastrointestinal tract. Results In this work we have explored the potential of B. coagulans MA-13 as a source of metabolites and enzymes to improve the digestibility and the nutritional value of food. A combination of mass spectrometry analysis with conventional biochemical approaches has been employed to unveil the intra- and extra- cellular glycosyl hydrolase (GH) repertoire of B. coagulans MA-13 under diverse growth conditions. The highest enzymatic activity was detected on β-1,4 and α-1,6-glycosidic linkages and the enzymes responsible for these activities were unambiguously identified as β-galactosidase (GH42) and α-galactosidase (GH36), respectively. Whilst the former has been found only in the cytosol, the latter is localized also extracellularly. The export of this enzyme may occur through a not yet identified secretion mechanism, since a typical signal peptide is missing in the α-galactosidase sequence. A full biochemical characterization of the recombinant β-galactosidase has been carried out and the ability of this enzyme to perform homo- and hetero-condensation reactions to produce galacto-oligosaccharides, has been demonstrated. Conclusions Probiotics which are safe for human use and are capable of producing high levels of both α-galactosidase and β-galactosidase are of great importance to the food industry. In this work we have proven the ability of B. coagulans MA-13 to over-produce these two enzymes thus paving the way for its potential use in treatment of gastrointestinal diseases.

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Section: Resultssupporting

confidence: 56%

Prebiotic properties of Bacillus coagulans MA-13: production of galactoside hydrolyzing enzymes and characterization of the transglycosylation properties of a GH42 β-galactosidase

et al. 2021

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show abstract

“…However, the electrophoretic mobility of this band (within the 130-180 KDa gel region) was identical to that identi ed as GH36 (Uniprot code: G2TQE8, Additional le 1) thus indicating that the enzymatic activity revealed by zymography, can be ascribed to the same protein. Besides our experimental evidences, the extracellular localization of the αgalactosidase has been previously described for another closely related B. coagulans strain [18,32] which was found to be able to grow on galactose-containing polymers (melibiose, ra nose, and stachyose) as well as for other soil microorganisms [33] and for Bacillus megaterium [34]. It is known that galactomannans are present in seeds of beans and in general RFOs (ra nose, stachyose, and verbascose) that contain α 1-6-linked galactose units, are particularly abundant in these legumes [9].…”

Section: Identi Cation Of the Hydrolytic Activities Through Mass Specsupporting

confidence: 75%

Prebiotic Properties of Bacillus Coagulans MA 13: Production of Galactoside Hydrolyzing Enzymes and Characterization of the Transglycosylation Properties of a GH42 β-Galactosidase

Aulitto

Strazzulli

Sansone

et al. 2021

Preprint

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BackgroundThe spore-forming lactic acid bacterium Bacillus coagulans MA-13 has been isolated from canned beans manufacturing and successfully employed for the sustainable production of lactic acid from lignocellulosic biomass. Among lactic acid bacteria, B. coagulans strains are generally recognized as safe (GRAS) for human consumption. Low-cost microbial production of industrially valuable products such as lactic acid and various enzymes devoted to the hydrolysis of oligosaccharides and lactose, is of great importance to the food industry. Specifically, α- and β-galactosidases are attractive for their ability to hydrolyze not-digestible galactosides present in the food matrix as well as in the human gastrointestinal tract.ResultsIn this work we have explored the potential of B. coagulans MA-13 as a source of metabolites and enzymes to improve the digestibility and the nutritional value of food. A combination of mass spectrometry analysis with conventional biochemical approaches has been employed to unveil the intra- and extra- cellular glycosyl hydrolase (GH) repertoire of B. coagulans MA-13 under diverse growth conditions. The highest enzymatic activity was detected on β-1,4 and α-1,6-glycosidic linkages and the enzymes responsible for these activities were unambiguously identified as a β-galactosidase (GH42) and α-galactosidase (GH36), respectively. Whilst the former has been found only in the cytosol, the latter is localized also extracellularly. The export of this enzyme may occur through a not yet identified secretion mechanism, since a typical signal peptide is missing in the α-galactosidase sequence. A full biochemical characterization of the recombinant β-galactosidase has been carried out and the ability of this enzyme to perform homo- and hetero-condensation reactions to produce galacto-oligosaccharides, has been demonstrated. ConclusionsProbiotics which are safe for human use and are capable of producing high levels of both α-galactosidase and β-galactosidase are of great importance to the food industry. In this work we have proven the ability of B. coagulans MA-13 to over-produce these two enzymes that are commonly used for treatment of gastrointestinal diseases. Moreover, B. coagulans MA-13 can be employed for an eco-friendly production of prebiotics from dairy food waste because of the ability of β-galactosidase to synthesize galacto-oligosaccharides from lactose.

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“…α-galactosidase can also facilitate the digestion of legumes, such as soybean, through removing galactosides such as raffinose and stachyose from their structures and enhancing the gelation capacities of galactomannans [ 74 ]. Several studies have reported on α-galactosidase produced by B. coagulans [ 62 , 63 ].…”

Section: Products Of B Coagulansmentioning

confidence: 99%

Potential Use of Bacillus coagulans in the Food Industry

Konuray

Erginkaya

2018

Foods

166

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Probiotic microorganisms are generally considered to beneficially affect host health when used in adequate amounts. Although generally used in dairy products, they are also widely used in various commercial food products such as fermented meats, cereals, baby foods, fruit juices, and ice creams. Among lactic acid bacteria, Lactobacillus and Bifidobacterium are the most commonly used bacteria in probiotic foods, but they are not resistant to heat treatment. Probiotic food diversity is expected to be greater with the use of probiotics, which are resistant to heat treatment and gastrointestinal system conditions. Bacillus coagulans (B. coagulans) has recently attracted the attention of researchers and food manufacturers, as it exhibits characteristics of both the Bacillus and Lactobacillus genera. B. coagulans is a spore-forming bacterium which is resistant to high temperatures with its probiotic activity. In addition, a large number of studies have been carried out on the low-cost microbial production of industrially valuable products such as lactic acid and various enzymes of B. coagulans which have been used in food production. In this review, the importance of B. coagulans in food industry is discussed. Moreover, some studies on B. coagulans products and the use of B. coagulans as a probiotic in food products are summarized.

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Biochemical Characterization of α-Galactosidase-Producing Thermophilic Bacillus coagulans KM-1

Cited by 5 publications

References 16 publications

Prebiotic properties of Bacillus coagulans MA-13: production of galactoside hydrolyzing enzymes and characterization of the transglycosylation properties of a GH42 β-galactosidase

Prebiotic properties of Bacillus coagulans MA-13: production of galactoside hydrolyzing enzymes and characterization of the transglycosylation properties of a GH42 β-galactosidase

Prebiotic Properties of Bacillus Coagulans MA 13: Production of Galactoside Hydrolyzing Enzymes and Characterization of the Transglycosylation Properties of a GH42 β-Galactosidase

Potential Use of Bacillus coagulans in the Food Industry

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