An α-<b>L</b>-Arabinofuranosidase Produced by Wild-Type<i>Streptomyces</i>sp. No. 17-1

Kaji, Akira; Sato, Masayuki; Tsutsui, Yasuo

doi:10.1080/00021369.1981.10864620

Cited by 7 publications

(4 citation statements)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The clone S. lividans IAF1 16 containing the abfA gene on the multicopy plasmid produced under the same conditions 2.41 units, corresponding to a 48-fold increase in enzyme production. This production level is amongst the highest reported in the literature (Kaji et al, 1981;Komae et al, 1982;Greve et al, 1984; Lee and Forsberg 1987;Hespell and O'Bryan, 1992;Tajana et al, 1992).…”

Section: Discussionmentioning

confidence: 57%

“…Thus the enzyme from Streptomyces sp. 17-1 hydrolyses arabinan, arabinoxylan or arabinogalactan (Kaji et al, 1981), whereas the AF from S. purpurascens is inactive towards these substrates, but is active on low-M, oligoarabinosides (Komae et al, 1982). S.…”

Section: Discussionmentioning

confidence: 99%

“…These enzymes have also been isolated from bacteria such as Bacillus subtilis (Weinstein and Albersheim, 1979), Clostridium acetobutylicum (Lee and Forsberg, 1987), Ruminococcus albus (Greve et al, 1984), Butyrivibrio fibrisolvens (Hespell and O'Bryan, 1992) and Streptomyces sp. (Kaji et al, 1981;Komae et al, 1982;Tajana et al, 1992). was obtained at 60°C and pH 6.0.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Purification and characterization of an α-l-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA)

Manin

Shareek

Morosoli

et al. 1994

Biochemical Journal

View full text Add to dashboard Cite

The gene encoding an alpha-L-arabinofuranosidase (abfA) was homologously cloned in Streptomyces lividans and its DNA sequence was determined. The enzyme was purified from the cytoplasm of the hyperproducing clone S. lividans IAF116. Its M(r) was estimated by gel filtration and found to be approx. 380,000. Since SDS/PAGE indicated a native protein of M(r) 69,000, it can be concluded that the native protein consists of several subunits of that size. The pI value was 4.6. The kinetic constants determined with p-nitrophenyl alpha-L-arabinofuranoside as substrate were a Vmax of 180 units/mg of protein and a Km of 0.6 mM. The specific activity of the purified enzyme on this substrate was 153 units/mg of protein. Optimal enzyme activity was obtained at 60 degrees C and pH 6.0. The enzyme cleaved p-nitrophenyl alpha-L-arabinofuranoside, but had no activity on a variety of other p-nitrophenyl glycosides, except on p-nitrophenyl beta-D-xylopyranoside. The enzyme showed no activity on oat-spelts (Avena sativa) xylan or arabinogalactan, but acted on beet (Beta) arabinan or arabinoxylan. Hydrolysis occurred on arabino-oligoxylosides obtained from oat-splets xylan after digestion with xylanases. Since S. lividans normally does not secrete arabinofuranosidase, this enzyme may play a role in the assimilation of arabinose moieties from arabinose-containing xylo-oligosaccharides generated by beta-xylosidases or xylanases.

show abstract

Section: Discussionmentioning

confidence: 57%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Purification and characterization of an α-l-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA)

Manin

Shareek

Morosoli

et al. 1994

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…These enzymes have also been isolated from bacteria such as Bacillus subtilis [12], Clostridium acetobutylicum [13], Butyri ibrio fibrisol ens [14], Bacillus stearothermophilus [15] and Streptomyces sp. [16][17][18]. abf genes coding for an intracellular enzyme [19] have been cloned from Pseudomonas fluorescens [20] and Streptomyces li idans.…”

Section: Introductionmentioning

confidence: 99%

New α-l-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme

Vincent

Shareck

Dupont

et al. 1997

Biochemical Journal

View full text Add to dashboard Cite

A fully secreted alpha-l-arabinofuranosidase was cloned from the homologous expression system of Streptomyces lividans. The gene, located upstream adjacent to the previously described xylanase A gene, was sequenced. It is divergently transcribed from the xlnA gene and the two genes are separated by an intercistronic region of 391nt which contains a palindromic AT-rich sequence. The deduced amino acid sequence of the protein shows that the enzyme contains a distinct catalytic domain which is linked to a specific xylan-binding domain by a linker region. The purified enzyme has a specific arabinofuranose-debranching activity on xylan from Gramineae, acts synergistically with the S. lividans xylanases and binds specifically to xylan. From small arabinoxylo-oligosides, it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well.

show abstract

Purification and characterization of a (1,4)-?-d-arabinoxylan arabinofuranohydrolase from Aspergillus awamori

Kormelink

Leeuwen

Wood³

et al. 1991

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

An enzyme able to split off arabinose sidechains from cereal arabinoxylans was isolated from a cell-free culture filtrate of Aspergillus awamori CMI 142717 containing milled oat straw as the carbon source. The enzyme was highly specific for arabinoxylans and, unlike other a-L-arabinofuranosidases reported in the literature, did not show any activity towards p-nitrophenyl a-L-arabinofuranoside, arabinans and arabinogalactans. This novel enzyme, which can be described as a (1,4)-fl-D-arabinoxylan arabinofuranohydrolase, had a molecular mass of 32 000 Da when determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and a specific activity of 22 units/mg on wheat arabinoxylan.

show abstract

An α-L-Arabinofuranosidase Produced by Wild-TypeStreptomycessp. No. 17-1

Cited by 7 publications

References 3 publications

Purification and characterization of an α-l-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA)

Purification and characterization of an α-l-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA)

New α-l-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme

Purification and characterization of a (1,4)-?-d-arabinoxylan arabinofuranohydrolase from Aspergillus awamori

Contact Info

Product

Resources

About