التفاصيل البيبلوغرافية
| العنوان: |
Molecular cloning, expression, and functional characterization of the β-agarase AgaB-4 from Paenibacillus agarexedens. |
| المؤلفون: |
Chen, Zeng-Weng, Lin, Hui-Jie, Huang, Wen-Cheng, Hsuan, Shih-Ling, Lin, Jiunn-Horng, Wang, Jyh-Perng |
| المصدر: |
AMB Express; 3/28/2018, Vol. 8 Issue 1, p1-1, 1p |
| مصطلحات موضوعية: |
PAENIBACILLUS, AGARASE, MOLECULAR cloning, SIGNAL peptides, NUCLEOTIDE sequencing |
| مستخلص: |
In this study, a β-agarase gene, agaB-4, was isolated for the first time from the agar-degrading bacterium Paenibacillus agarexedens BCRC 17346 by using next-generation sequencing. agaB-4 consists of 2652 bp and encodes an 883-amino acid protein with an 18-amino acid signal peptide. agaB-4 without the signal peptide DNA was cloned and expressed in Escherichia coli BL21(DE3). His-tagged recombinant AgaB-4 (rAgaB-4) was purified from the soluble fraction of E. coli cell lysate through immobilized metal ion affinity chromatography. The optimal temperature and pH of rAgaB-4 were 55 °C and 6.0, respectively. The results of a substrate specificity test showed that rAgaB-4 could degrade agar, high-melting point agarose, and low-melting point agarose. The Vmax and Km of rAgaB-4 for low-melting point agarose were 183.45 U/mg and 3.60 mg/mL versus 874.61 U/mg and 9.29 mg/mL for high-melting point agarose, respectively. The main products of agar and agarose hydrolysis by rAgaB-4 were confirmed to be neoagarotetraose. Purified rAgaB-4 can be used in the recovery of DNA from agarose gels and has potential application in agar degradation for the production of neoagarotetraose. [ABSTRACT FROM AUTHOR] |
|
Copyright of AMB Express is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| قاعدة البيانات: |
Complementary Index |
Find this article in full text from Springer Verlag. 
Full Text Finder