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Item
Characterization of a thermostable feruloyl esterase B from Talaromyces cellulolyticus
https://aist.repo.nii.ac.jp/records/2001838
https://aist.repo.nii.ac.jp/records/200183816178dc4-4c55-4e69-9981-0bd1d3c41b5b
| Item type | Research Data (v9)(1) | |||||||||||||||
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| PubDate | 2015-01-01 | |||||||||||||||
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| Title | Characterization of a thermostable feruloyl esterase B from Talaromyces cellulolyticus | |||||||||||||||
| Language | en | |||||||||||||||
| Description of data | ||||||||||||||||
| Description Type | Abstract | |||||||||||||||
| Description | A carbohydrate esterase, hemicellulase accessory enzyme, catalyzes the de-O or de-N-acylation of substituted saccharides and has been expected to be an industrially important enzyme for biomass saccharification. A feruloyl esterase (EC. 3.1.1.73) belonging to the carbohydrate esterase catalyses the hydrolysis of the 4-hydroxy-3-methoxycinnamoyl (feruloyl) group from an esterified sugars and is one of the predominant carbohydrate esterases. In the genome data base of fungal Talaromyses cellulolyticus (formerly known as Acremonium cellulolyticus) (unpublished data), the gene encoding a putative carbohydrate esterase was found. The gene contains an open reading frame of 1,071 bp encoding a protein with molecular mass of 37,689 Da. From the sequence analysis, it was suggested that the enzyme is including the conserved catalytic triad (Ser136, Asp220 and His276) of serine esterases and consists of putative three parts that are catalytic domain, linker domain and cellulose-binding module. The recombinant enzyme was prepared with the homologous expression system using T. cellulolyticus Y212 derived the CF-2612 strain and characterized. The purified enzyme exhibited the hydrolytic activity toward methyl ferulate, rice husk, and bagasse. According to HPLC assays, it was elucidated that the enzyme released ferulic acids from rice husk, but not so much ferulic acids as p-coumaric acids from bagasse. The optimum temperature and pH of the enzyme were estimated to be over 65 °C and 6.0, respectively. The melting temperature (Tm) of the enzyme was determined to be 70 °C by differential scanning calorimetry (DSC). From these results, it was clarified that T. cellulolyticus can produce a theremophilic feruloyl esterase and this enzyme is expected to be industrially used for biomass saccharification. | |||||||||||||||
| Language | en | |||||||||||||||
| Author (Creator) name |
渡邊 真宏
× 渡邊 真宏
× 吉田エリカ
× 深田寛郎
× 十倉充範
× 井上 宏之
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| Access Rights | ||||||||||||||||
| Access Rights | open access | |||||||||||||||
| Access Rights URI | http://purl.org/coar/access_right/c_abf2 | |||||||||||||||
| APC | ||||||||||||||||
| APC | Not required | |||||||||||||||
| Rights Holder | ||||||||||||||||
| Right Holder Name | 渡邊 真宏 | |||||||||||||||
| Language | en | |||||||||||||||
| Publisher | ||||||||||||||||
| Publisher | 日本農芸化学会 | |||||||||||||||
| Language | en | |||||||||||||||
| Date | ||||||||||||||||
| Date | 2015-01-01 | |||||||||||||||
| Date Type | Issued | |||||||||||||||
| Language | ||||||||||||||||
| Language | eng | |||||||||||||||
| Resource Type | ||||||||||||||||
| Resource Type Identifier | http://purl.org/coar/resource_type/c_6501 | |||||||||||||||
| Resource Type | journal article | |||||||||||||||
| Identifier | ||||||||||||||||
| Identifier | 10.1080/09168451.2015.1058700 | |||||||||||||||
| Identifier Type | DOI | |||||||||||||||
| Relation | ||||||||||||||||
| Relation Type | isVersionOf | |||||||||||||||
| Identifier Type | URI | |||||||||||||||
| Related Identifier | http://www.tandfonline.com/doi/full/10.1080/09168451.2015.1058700 | |||||||||||||||
| Language | ja | |||||||||||||||
| Related Title | 関連 URI | |||||||||||||||
| Source Title | ||||||||||||||||
| Source Title | BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | |||||||||||||||
| Language | en | |||||||||||||||
| Volume Number | ||||||||||||||||
| Volume | 79 | |||||||||||||||
| Issue Number | ||||||||||||||||
| Issue | 11 | |||||||||||||||
| Page Start | ||||||||||||||||
| Start Page | 1845 | |||||||||||||||
| Page End | ||||||||||||||||
| End Page | 1851 | |||||||||||||||
