Biodegradation of Alginate, Xanthan, and Gellan

Hashimoto, Wataru; Mishima, Yumiko; Miyake, Osamu; Nankai, Hirokazu; Momma, Keiko; Murata, Kousaku

doi:10.1002/3527600035.bpol9009

Cited by 6 publications

(11 citation statements)

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“…It is produced by a number of animal tissues, plants, fungi, bacteria and bacteriophage (Hashimoto et al, 2003). The physiological role of a-L-rhamnosidase is not well understood but is probably linked to the broad distribution of L-rhamnose as a component in bacterial and plant cell walls, glycosides, biofilms and glycolipids (Bader et al, 1998;Giavasis et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Physiological and biochemical characterization of the two α-l-rhamnosidases of Lactobacillus plantarum NCC245

et al. 2009

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This work is believed to be the first report on the physiological and biochemical characterization of a-L-rhamnosidases in lactic acid bacteria. A total of 216 strains representing 37 species and eight genera of food-grade bacteria were screened for a-L-rhamnosidase activity. The majority of positive bacteria (25 out of 35) were Lactobacillus plantarum strains, and activity of the L. plantarum strain NCC245 was examined in more detail. The analysis of a-L-rhamnosidase activity under different growth conditions revealed dual regulation of the enzyme activity, involving carbon catabolite repression and induction: the enzyme activity was downregulated by glucose and upregulated by L-rhamnose. The expression of the two a-L-rhamnosidase genes rhaB1 and rhaB2 and two predicted permease genes rhaP1 and rhaP2, identified in a probable operon rhaP2B2P1B1, was repressed by glucose and induced by L-rhamnose, showing regulation at the transcriptional level. The two a-L-rhamnosidase genes were overexpressed and purified from Escherichia coli. RhaB1 activity was maximal at 50 6C and at neutral pH and RhaB2 maximal activity was detected at 60 6C and at pH 5, with high residual activity at 70 6C. Both enzymes showed a preference for the a-1,6 linkage of L-rhamnose to b-D-glucose, hesperidin and rutin being their best substrates, but, surprisingly, no activity was detected towards the a-1,2 linkage in naringin under the tested conditions. In conclusion, we identified and characterized the strain L. plantarum NCC245 and its two a-L-rhamnosidase enzymes, which might be applied for improvement of bioavailability of health-beneficial polyphenols, such as hesperidin, in humans.

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Section: Introductionmentioning

confidence: 99%

Physiological and biochemical characterization of the two α-l-rhamnosidases of Lactobacillus plantarum NCC245

et al. 2009

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“…7) A1-II 0 of strain A1 31) and function-unknown protein PA1167 (25 kDa) of P. aeruginosa 38) have been identified as endotype family PL-7 alginate lyases. PA1167 consists of two -sheets with 15 -strands and threehelices, which constitute a glove-like -sandwich structure.…”

Section: Family Pl-7 Lyasesmentioning

confidence: 99%

“…6,7) The three endotype alginate lyases originate from a single gene aly; i.e., A1-I is autocatalytically processed into A1-II and A1-III, specific to polyG and polyM respectively, 7) and release unsaturated di-, tri-, and tetrasaccharides from alginate. All unsaturated oligosaccharides thus produced are then degraded by an exotype lyase into constituent monosaccharides, which are nonenzymatically converted to -keto acids.…”

Section: Alginate Lyasesmentioning

confidence: 99%

“…Due to this structural heterogeneity, bacterial exopolysaccharides and their depolymerization products are expected to show potent biochemical and biotechnological characteristics. Enzymes acting on bacterial polysaccharides, including alginate, xanthan, and gellan, 7) should be useful in the molecular design of poly-and oligosaccharides with novel biotechnological functions. Although some of the oligosaccharides produced by polysaccharide lyases are now applicable in the food, agricultural, chemical, and medical industries, 7,84) this field has not yet matured.…”

Section: Biomass Engineeringmentioning

confidence: 99%

“…2). 6,7) In case of alginate engulfment, dynamic structural and functional fluctuations leading to the formation of the pit occur on the cell surface of strain A1. This indicates that substantial structural and functional fluctuations occur frequently on the cell surface in other than extreme cases Cells were cultured in the presence of alginate for (upper, from left) 0, 7, and 10 h, and (lower, left) 24 h. The magnified picture of the pit (lower, middle, and right) indicates the disappearance and rearrangement of pleat molecules and substantial accumulation of alginate gel particles.…”

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confidence: 99%

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Superchannel of Bacteria: Biological Significance and New Horizons

Murata

Kawai

Mikami

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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Degradation of rice bran hemicellulose by Paenibacillus sp. strain HC1: gene cloning, characterization and function of β-D-glucosidase as an enzyme involved in degradation

et al. 2005

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A bacterium (strain HC1) capable of assimilating rice bran hemicellulose was isolated from a soil and identified as belonging to the genus Paenibacillus through taxonomical and 16S rDNA sequence analysis. Strain HC1 cells grown on rice bran hemicellulose as a sole carbon source inducibly produced extracellular xylanase and intracellular glycosidases such as beta-D-glucosidase and beta-D-arabinosidase. One of them, beta-D-glucosidase, was further analyzed. A genomic DNA library of the bacterium was constructed in Escherichia coli and gene coding for beta-D-glucosidase was cloned by screening for beta-D-glucoside-degrading phenotype in E. coli cells. Nucleotide sequence determination indicated that the gene for the enzyme contained an open reading frame consisting of 1,347 bp coding for a polypeptide with a molecular mass of 51.4 kDa. The polypeptide exhibits significant homology with other bacterial beta-D-glucosidases and belongs to glycoside hydrolase family 1. Beta-D-Glucosidase purified from E. coli cells was a monomeric enzyme with a molecular mass of 50 kDa most active at around pH 7.0 and 37 degrees C. Strain HC1 glycosidases responsible for degradation of rice bran hemicellulose are expected to be useful for structurally determining and molecularly modifying rice bran hemicellulose and its derivatives.

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Biodegradation of Alginate, Xanthan, and Gellan

Abstract: Introduction Historical Outline Alginate Xanthan Gellan Alginate Depolymerization Alginate‐assimilating Bacterium Genes Responsible for Uptake of Alginate Enzymatic Depolymerization System for Alginate i… Show more

Cited by 6 publications

References 82 publications

Physiological and biochemical characterization of the two α-l-rhamnosidases of Lactobacillus plantarum NCC245

Physiological and biochemical characterization of the two α-l-rhamnosidases of Lactobacillus plantarum NCC245

Superchannel of Bacteria: Biological Significance and New Horizons

Degradation of rice bran hemicellulose by Paenibacillus sp. strain HC1: gene cloning, characterization and function of β-D-glucosidase as an enzyme involved in degradation

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