Thermal Stabilization of Aspergillus Phytase by L-Arginine
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Ryu, S | ko |
| dc.contributor.author | Park, Tae Gwan | ko |
| dc.date.accessioned | 2013-02-27T15:04:17Z | - |
| dc.date.available | 2013-02-27T15:04:17Z | - |
| dc.date.created | 2012-02-06 | - |
| dc.date.created | 2012-02-06 | - |
| dc.date.created | 2012-02-06 | - |
| dc.date.issued | 1998-05 | - |
| dc.identifier.citation | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING, v.3, no.0, pp.32 - 34 | - |
| dc.identifier.issn | 1226-8372 | - |
| dc.identifier.uri | http://hdl.handle.net/10203/69233 | - |
| dc.description.abstract | Phytase from Aspergillus species is a very heat unstable enzyme which inactivates to a great extent during the thermal processing of animal feed formulation. Various protein stabilization additives were tested to improve its heat stability. Among them, a basic amino acid, L-arginine remarkably increased the thermal stability of phytase in an aqueous solution state. | - |
| dc.language | English | - |
| dc.publisher | KOREAN SOC BIOTECHNOLOGY & BIOENGINEERING | - |
| dc.title | Thermal Stabilization of Aspergillus Phytase by L-Arginine | - |
| dc.type | Article | - |
| dc.identifier.scopusid | 2-s2.0-54649083140 | - |
| dc.type.rims | ART | - |
| dc.citation.volume | 3 | - |
| dc.citation.issue | 0 | - |
| dc.citation.beginningpage | 32 | - |
| dc.citation.endingpage | 34 | - |
| dc.citation.publicationname | BIOTECHNOLOGY AND BIOPROCESS ENGINEERING | - |
| dc.identifier.doi | 10.1007/BF02932480 | - |
| dc.contributor.localauthor | Park, Tae Gwan | - |
| dc.contributor.nonIdAuthor | Ryu, S | - |
| dc.description.isOpenAccess | N | - |
- Appears in Collection
- BS-Journal Papers(저널논문)
- Files in This Item
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.