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Literature summary for 3.2.1.8 extracted from

  • Sriyapai, T.; Somyoonsap, P.; Matsui, K.; Kawai, F.; Chansiri, K.
    Cloning of a thermostable xylanase from Actinomadura sp. S14 and its expression in Escherichia coli and Pichia pastoris (2011), J. Biosci. Bioeng., 111, 528-536.
    View publication on PubMed
Search for more literature for 3.2.1.8

Cloned(Commentary)

Cloned (Comment) Organism
gene xynS14, DNA and amino acid sequence determination and analysis, expression of His-tagged XynS14 in Escherichia coli and Pichia pastoris Actinomadura sp.

General Stability

General Stability Organism
sorbitol at 90% and glycerol at 50% stabilize the enzyme Actinomadura sp.

Organism

Organism UniProt Comment Textmining
Actinomadura sp.
-
 isolated from compost in Thailand, gene xynS14
-
Actinomadura sp. S14
-
 isolated from compost in Thailand, gene xynS14
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein XynS14 is expressed in Pichia pastoris as glycoproteins with different glycosylation levels at four N-glycosylation sites Actinomadura sp.

Purification (Commentary)

Purification (Comment) Organism
recombinant XynS14 from Pichia pastoris by ultrafiltration and gel filtration, recombinant His-tagged XynS14 from Escherichia coli by heat treatment, nickel affinity chromatography, and gel filtration Actinomadura sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beech wood xylan + H2O
-
 Actinomadura sp. ?
-
 ?
beech wood xylan + H2O
-
 Actinomadura sp. S14 ?
-
 ?
birch wood xylan + H2O
-
 Actinomadura sp. ?
-
 ?
birch wood xylan + H2O
-
 Actinomadura sp. S14 ?
-
 ?
additional information substrates are oat spelt xylan, corncob, corn hull, cane bagasse, and rice straw. Purified recombinant XynS14 shows more endo-1,4-beta-xylanase activity on xylan and xylooligosaccharides than on xylotriose Actinomadura sp. ?
-
 ?
additional information substrates are oat spelt xylan, corncob, corn hull, cane bagasse, and rice straw. Purified recombinant XynS14 shows more endo-1,4-beta-xylanase activity on xylan and xylooligosaccharides than on xylotriose Actinomadura sp. S14 ?
-
 ?
oat spelt xylan + H2O
-
 Actinomadura sp. ?
-
 ?
oat spelt xylan + H2O
-
 Actinomadura sp. S14 ?
-
 ?

Synonyms

Synonyms Comment Organism
endo-1,4-beta-xylanase
-
 Actinomadura sp.
xylanase
-
 Actinomadura sp.
XynS14
-
 Actinomadura sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
 recombinant XynS14 Actinomadura sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60 70 purified recombinant XynS14s, 12 h, completely stable Actinomadura sp.
80
-
 XynS14 expressed from Pichia pastoris shows 50% remaining activity after 2 h, the enzyme expressed from Escherichia coli shows 30% remaining activity. In the presence of sorbitol at 90% and glycerol at 50%, the enzyme retains approximately 70% and 80% activity, respectively, at 80°C for 4 h Actinomadura sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 recombinant XynS14 Actinomadura sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
4
-
 XynS14 expressed from Pichia pastoris shows 50% remaining activity after 1 h, the enzyme expressed from Escherichia coli shows 10% remaining activity after 30 min Actinomadura sp.
5 11 purified recombinant XynS14s, stable Actinomadura sp.

Expression

Organism Comment Expression
Actinomadura sp. the enzyme is induced by xylan-containing agriculture wastes and oat spelt xylan up

General Information

General Information Comment Organism
additional information specific activity of purified recombinant XynS14, expressed in Pichia pastoris, is 2.4fold higher than recombinant XynS14, expressed in Escherichia coli Actinomadura sp.