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Literature summary for 3.2.1.8 extracted from
- Cloning, sequencing, and expression of the gene encoding a multidomain endo-beta-1,4-Xylanase from Paenibacillus curdlanolyticus B-6, and characterization of the recombinant enzyme (2009), J. Microbiol. Biotechnol., 19, 277-285.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | Xyn10A is a modular xylanase comprising nine domains, i.e., three family 22 carbohydrate-binding modules (CBMs), a family 10 catalytic domain of glycosyl hydrolases (xylanase), a family 9 CBM, a glycine-rich region, and three surface layer homology (SLH) domains. The CBMs of Xyn10A play an important role in the hydrolysis of plant cell walls | Paenibacillus curdlanolyticus |
Application
| Application | Comment | Organism |
|---|---|---|
| industry | purified recombinant Xyn10A is a useful candidate for producing xylooligosaccharides as thickeners, fat substitutes, and antifreeze food additives in the food industry | Paenibacillus curdlanolyticus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| pUC19 plasmid, carrying the 10-kb HindIII fragment containing the xylanase gene expressed in Escherichia coli DH5alpha | Paenibacillus curdlanolyticus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | removal of the CBMs from Xyn10A strongly reduces the ability of plant cell wall hydrolysis | Paenibacillus curdlanolyticus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 142700 | - |
sequence analysis | Paenibacillus curdlanolyticus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paenibacillus curdlanolyticus | B1A3N2 | - |
- |
| Paenibacillus curdlanolyticus B-6 | B1A3N2 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| by a single step of affinity purification on avicel, 139.4fold with a 38.1% yield | Paenibacillus curdlanolyticus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.7 | - |
crude extract | Paenibacillus curdlanolyticus |
| 97.6 | - |
139.4fold purifed enzyme | Paenibacillus curdlanolyticus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-cellulose + H2O | high affinity, affinity is slightly greater for celluloses than for insoluble xylans and chitin | Paenibacillus curdlanolyticus | ? | - |
? |  |
| alpha-cellulose + H2O | high affinity, affinity is slightly greater for celluloses than for insoluble xylans and chitin | Paenibacillus curdlanolyticus B-6 | ? | - |
? | |
| avicel + H2O | high affinity | Paenibacillus curdlanolyticus | ? | - |
? | |
| avicel + H2O | high affinity | Paenibacillus curdlanolyticus B-6 | ? | - |
? | |
| birchwood xylan + H2O | high affinity, hydrolyzes birchwood xylan (hard wood) more effectively than oat spelt xylan (soft wood) | Paenibacillus curdlanolyticus | ? | - |
? | |
| cell wall fragment + H2O | Xyn10A containing three SLH domains at its C-terminus can bind to cell wall fragments significantly (32%) | Paenibacillus curdlanolyticus | ? | - |
? | |
| chitin + H2O | high affinity | Paenibacillus curdlanolyticus | ? | - |
? | |
| chitin + H2O | high affinity | Paenibacillus curdlanolyticus B-6 | ? | - |
? | |
| additional information | can effectively hydrolyze agricultural wastes, e.g., corn cob, corn hull, rice husk (which has a strong structure and is normally not easy to hydrolyze), rice straw, and bagasse | Paenibacillus curdlanolyticus | ? | - |
? | |
| additional information | can effectively hydrolyze agricultural wastes, e.g., corn cob, corn hull, rice husk (which has a strong structure and is normally not easy to hydrolyze), rice straw, and bagasse | Paenibacillus curdlanolyticus B-6 | ? | - |
? | |
| oat spelt xylan + H2O | high affinity | Paenibacillus curdlanolyticus | ? | - |
? | |
| starch + H2O | some affinity for polysaccharides that do not contain beta-1,4 linkages, e.g., starches from potato and wheat | Paenibacillus curdlanolyticus | ? | - |
? | |
| starch + H2O | some affinity for polysaccharides that do not contain beta-1,4 linkages, e.g., starches from potato and wheat | Paenibacillus curdlanolyticus B-6 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| endo-beta-1,4-xylanase | - |
Paenibacillus curdlanolyticus |
| xylanase | - |
Paenibacillus curdlanolyticus |
| Xyn10A | - |
Paenibacillus curdlanolyticus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
- |
Paenibacillus curdlanolyticus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Paenibacillus curdlanolyticus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
- |
Paenibacillus curdlanolyticus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5 | 8 | still 80% stability at pH 9.0 | Paenibacillus curdlanolyticus |
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