Purification and Characterization of<scp>D</scp>-Xylose Isomerase from<i>Bifidobacterium adolescentis</i>

Kawai, Yoshifumi; Konishi, Hiroaki; Horitsu, Hiroyuki; Sakurai, Hiroaki; Takamizawa, Kazuhiro; Suzuki, Tomohiko; Kawai, Kazuhiro

doi:10.1271/bbb.58.691

Cited by 10 publications

(6 citation statements)

References 7 publications

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Section: Discussionsupporting

confidence: 91%

“…In the present study, the maximum enzyme activity of GI produced by S. albaduncus was observed in the presence of the combination of Mg 2+ and Co 2+ ions (5 mM). The reducing effects of some metal ions such as Ag 1+ , Hg 2+ , Cu 2+ , Zn 2+ , Ni 2+ and Ca 2+ on the GI activity observed in the present study was also reported by other investigators Chen and Anderson (1979), Smith et al (1991) and Kawai et al (1994).…”

Section: Discussionsupporting

confidence: 91%

“…However, higher optimum temperature (80°C) for GI activity was observed in the study of Azin et al (1997) and Srivastava et al (2010). On the other hand, lower temperature (60°C) was the optimum for the activity of GI produced by Lactobacillus xylosus (Kawai et al, 1994).…”

Section: Discussionmentioning

confidence: 94%

“…The enzyme homogeneity in the final product was confirmed by formation of single protein band of estimated molecular weight 54 kDa in the SDS-PAGE. Kawai et al (1994) purified GI enzymes from culture supernatant of Bifidobacterium adolescent with estimated molecular weight of 53 kDa, while the GI enzyme produced by Streptomyces flavogriseus has a smaller molecular weight of 43 kDa (Chen and Anderson, 1979).…”

Section: Discussionmentioning

confidence: 99%

“…A suitable GI activity can be obtained over a pH range from 6 to 8 (Kawai et al, 1994). In the present study, a promising enzyme activity was observed over the range of 6.5 to 8, with optimum level at pH 7 which is in agreement with that reported by Kawai et al (1994). While, slight alkaline condition, pH 7.5 and 8, are the optimum for the activity of GI enzyme produced by Streptomyces flavogriseus and Streptomyces phaeochromogenes NRRL B-3559, respectively (Standberg and Smiley, 1971;Chen and Anderson, 1979).…”

Section: Discussionmentioning

confidence: 99%

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Purification, characterization and immobilization of glucose isomerase from Streptomyces albaduncus

Mahmoud¹,

Asif²,

Hani³

2013

Afr. J. Microbiol. Res.

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Glucose isomerase produced from Streptomyces albaduncus was purified to homogeneity by ammonium sulphate precipitation, followed by ion exchange DEAE-cellulose chromatography, and finally on DEAE-Sephadex A-50 chromatography. The molecular weight of the purified enzyme was estimated to be 54 kDa by sodium dodecyl sulphate polyacrylamide gel electrophresis (SDS-PAGE). The final preparation by the purification procedure had 10.3% final activity recovery and 13.3-fold purification. The optimum pH and temperature for GI activity were 7 and 70°C, respectively. In addition, the presence of the combination of Mg 2+ and Co 2+ ions (5 mM) improve the GI activity. Partially purified GI enzyme was immobilized by cross-linking with gluteraldahyde, adsorption on DEAE-Cellulose, and entrapment into polyacrylamide. Immobilization of GI enzyme caused sight decrease (3-19% reduction) in the enzymatic activity as compared to that of the non-immobilized enzyme. The maximum enzymatic activity (97%) and stability (88%) was obtained in the immobilized enzyme prepared by entrapment into polyacrylamide.

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Section: Discussionsupporting

confidence: 91%

Section: Discussionsupporting

confidence: 91%

Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 3 more Smart Citations

Purification, characterization and immobilization of glucose isomerase from Streptomyces albaduncus

Mahmoud¹,

Asif²,

Hani³

2013

Afr. J. Microbiol. Res.

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Bifidobacterium carbohydrases‐their role in breakdown and synthesis of (potential) prebiotics

Broek

Hinz

Beldman

et al. 2008

Molecular Nutrition Food Res

145

109

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There is an increasing interest to positively influence the human intestinal microbiota through the diet by the use of prebiotics and/or probiotics. It is anticipated that this will balance the microbial composition in the gastrointestinal tract in favor of health promoting genera such as Bifidobacterium and Lactobacillus. Carbohydrates like non-digestible oligosaccharides are potential prebiotics. To understand how these bacteria can grow on these carbon sources, knowledge of the carbohydrate-modifying enzymes is needed. Little is known about the carbohydrate-modifying enzymes of bifidobacteria. The genome sequence of Bifidobacterium adolescentis and Bifidobacterium longum biotype longum has been completed and it was observed that for B. longum biotype longum more than 8% of the annotated genes were involved in carbohydrate metabolism. In addition more sequence data of individual carbohydrases from other Bifidobacterium spp. became available. Besides the degradation of (potential) prebiotics by bifidobacterial glycoside hydrolases, we will focus in this review on the possibilities to produce new classes of non-digestible oligosaccharides by showing the presence and (transglycosylation) activity of the most important carbohydrate modifying enzymes in bifidobacteria. Approaches to use and improve carbohydrate-modifying enzymes in prebiotic design will be discussed.

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Application of a compatible xylose isomerase in simultaneous bioconversion of glucose and xylose to ethanol

Chandrakant

Bisaria

2000

Biotechnol. Bioprocess Eng.

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Purification and Characterization ofD-Xylose Isomerase fromBifidobacterium adolescentis

Cited by 10 publications

References 7 publications

Purification, characterization and immobilization of glucose isomerase from Streptomyces albaduncus

Purification, characterization and immobilization of glucose isomerase from Streptomyces albaduncus

Bifidobacterium carbohydrases‐their role in breakdown and synthesis of (potential) prebiotics

Application of a compatible xylose isomerase in simultaneous bioconversion of glucose and xylose to ethanol

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