Purification and properties of a galacto- and gluco-oligosaccharide-producing β-glycosidase from Rhodotorula minuta IFO879

Onishi, Norimasa; Tanaka, Takashi

doi:10.1016/s0922-338x(97)86979-6

Cited by 42 publications

(24 citation statements)

References 9 publications

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“…The yield of GaOS by ␤-GalI was higher than those reported using the ␤-galactosidase of Thermus aquaticus (2), B. bifidum (10), Bacillus circulans (34), Aspergillus oryzae (44), and Kluyveromyces lactis (23), which were less than 42 mg/ml. The total concentration of GaOS (mainly tri-and tetrasaccharides) produced by the yeast Rhodotorula minuta ␤-galactosidase was about 78 mg/ml (40), which was lower than the total GaOS but higher than the concentration (66 mg/ml) of tri-and tetrasaccharides (Fig. 5, peaks 6 and 7) produced by ␤-GalI.…”

Section: Discussionmentioning

confidence: 80%

“…The trisaccharide produced by ␤-galactosidase from B. bifidum was also identified as 3Ј-galactosyl-lactose (11). However, 4Ј-galactosyl-lactose and 6Ј-galactosyl-lactose were reported to be preferentially formed during the transgalactosylation reactions (1,39,40,62), and several ␤-galactosidases were found to produce more than one type of GaOS (1,57,62). Comparing the prebiotic effects of 3Ј-galactosyl-lactose, 4Ј-galactosyl-lactose, and 6Ј-galactosyl-lactose is essential to determine their relative values as nutraceutical additives for humans or animals.…”

Section: Discussionmentioning

confidence: 99%

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Molecular and Biochemical Analysis of Two β-Galactosidases fromBifidobacterium infantisHL96

Hung

Xia

et al. 2001

Appl Environ Microbiol

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Two genes encoding ␤-galactosidase isoenzymes, ␤-galI and ␤-galIII, from Bifidobacterium infantis HL96 were revealed on 3.6-and 2.4-kb DNA fragments, respectively, by nucleotide sequence analysis of the two fragments. ␤-galI (3,069 bp) encodes a 1,022-amino-acid (aa) polypeptide with a predicted molecular mass of 113 kDa. A putative ribosome binding site and a promoter sequence were recognized at the 5 flanking region of ␤-galI.

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Section: Discussionmentioning

confidence: 80%

Section: Discussionmentioning

confidence: 99%

Molecular and Biochemical Analysis of Two β-Galactosidases fromBifidobacterium infantisHL96

Hung

Xia

et al. 2001

Appl Environ Microbiol

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“…5A) and increased the total yield of GOS to ϳ30%. Even though the comparison of the results reported for various enzymes would be difficult due to different reaction conditions used in other studies, the total amount of GOS produced by GP643.3 seemed to be comparable to those for the relevant enzymes derived from Bifidobacterium bifidum (29%) (9), Sterigmatomyces elviae CBS8119 (34%) (24), Rhodotorula minuta IFO879 (35%) (25), and Enterobacter agglomerans 38% (20).…”

Section: Discussionmentioning

confidence: 80%

Evolved β-Galactosidases from Geobacillus stearothermophilus with Improved Transgalactosylation Yield for Galacto-Oligosaccharide Production

Placier

Watzlawick

Rabiller

et al. 2009

Appl Environ Microbiol

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A mutagenesis approach was applied to the ␤-galactosidase BgaB from Geobacillus stearothermophilus KVE39 in order to improve its enzymatic transglycosylation of lactose into oligosaccharides. A simple screening strategy, which was based on the reduction of the hydrolysis of a potential transglycosylation product (lactosucrose), provided mutant enzymes possessing improved synthetic properties for the autocondensation product from nitrophenyl-galactoside and galacto-oligosaccharides (GOS) from lactose. The effects of the mutations on enzyme activity and kinetics were determined. An change of one arginine to lysine (R109K) increased the oligosaccharide yield compared to that for the wild-type BgaB. Subsequently, saturation mutagenesis at this position demonstrated that valine and tryptophan further increased the transglycosylation performance of BgaB. During the transglycosylation reaction with lactose of the evolved ␤-galactosidases, a major trisaccharide was formed. Its structure was characterized as ␤-D-galactopyranosyl-(133)-␤-D-galactopyranosyl-(134)-D-glucopyranoside (3-galactosyl-lactose). At the lactose concentration of 18% (wt/vol), this trisaccharide was obtained in yields of 11.5% (wt/wt) with GP21 (BgaB R109K), 21% with GP637.2 (BgaB R109V), and only 2% with the wild-type BgaB enzyme. GP643.3 (BgaB R109W) was shown to be the most efficient mutant, with a 3-galactosyl-lactose production of 23%.

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“…However, CreA homologs have been detected in all basidiomycete genomes sequenced so far (184). In line with the ascomycetes, various basidiomycetes, such as the white rot fungus Trametes (Coriolus) versicolor, the litter decomposers A. bisporus and V. volvacea, the phytopathogen S. rolfsii, and the basidiomycete yeast Rhodotorula minuta, have CAZyme-encoding genes that are repressed by glucose and other monosaccharides (89,(185)(186)(187)(188). Some CAZymeencoding genes are also repressed by monosaccharides that seem unrelated to the enzymes that these genes encode.…”

Section: Repression Of Gene Expression In Basidiomycetesmentioning

confidence: 99%

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Rytioja

Hildén

Yuzon

et al. 2014

Microbiol Mol Biol Rev

348

287

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SUMMARY Basidiomycete fungi subsist on various types of plant material in diverse environments, from living and dead trees and forest litter to crops and grasses and to decaying plant matter in soils. Due to the variation in their natural carbon sources, basidiomycetes have highly varied plant-polysaccharide-degrading capabilities. This topic is not as well studied for basidiomycetes as for ascomycete fungi, which are the main sources of knowledge on fungal plant polysaccharide degradation. Research on plant-biomass-decaying fungi has focused on isolating enzymes for current and future applications, such as for the production of fuels, the food industry, and waste treatment. More recently, genomic studies of basidiomycete fungi have provided a profound view of the plant-biomass-degrading potential of wood-rotting, litter-decomposing, plant-pathogenic, and ectomycorrhizal (ECM) basidiomycetes. This review summarizes the current knowledge on plant polysaccharide depolymerization by basidiomycete species from diverse habitats. In addition, these data are compared to those for the most broadly studied ascomycete genus, Aspergillus , to provide insight into specific features of basidiomycetes with respect to plant polysaccharide degradation.

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Purification and properties of a galacto- and gluco-oligosaccharide-producing β-glycosidase from Rhodotorula minuta IFO879

Cited by 42 publications

References 9 publications

Molecular and Biochemical Analysis of Two β-Galactosidases fromBifidobacterium infantisHL96

Molecular and Biochemical Analysis of Two β-Galactosidases fromBifidobacterium infantisHL96

Evolved β-Galactosidases from Geobacillus stearothermophilus with Improved Transgalactosylation Yield for Galacto-Oligosaccharide Production

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

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