Reference - Detail
| RRC ID | 66715 |
|---|---|
| Author | Ramos KRM, Valdehuesa KNG, Bañares AB, Nisola GM, Lee WK, Chung WJ. |
| Title | Overexpression and characterization of a novel GH16 β-agarase (Aga1) from Cellulophaga omnivescoria W5C. |
| Journal | Biotechnol Lett |
| Abstract |
OBJECTIVE:To identify and characterize a new β-agarase from Cellulophaga omnivescoria W5C capable of producing biologically-active neoagarooligosaccharides from agar. RESULTS:The β-agarase, Aga1, has signal peptides on both N- and C-terminals, which are involved in the type IX secretion system. It shares 75% protein sequence identity with AgaD from Zobellia galactanivorans and has a molecular weight of 54 kDa. Biochemical characterization reveals optimum agarolytic activities at pH 7-8 and temperature 30-45 °C. Aga1 retains at least 33% activity at temperatures lower than the sol-gel transition state of agarose. Metal ions are generally not essential, but calcium and potassium enhance its activity whereas iron and zinc are inhibitory. Finally, hydrolysis of agarose with Aga1 yields neoagarotetraose, neoagarohexaose, and neoagarooctaose. CONCLUSIONS:Aga1 displays unique traits such as moderate psychrophilicity, stability, and synergy with other agarases, which makes it an excellent candidate for biosynthetic production of neoagarooligosaccharides from agar. |
| Volume | 42(11) |
| Pages | 2231-2238 |
| Published | 2020-11-1 |
| DOI | 10.1007/s10529-020-02933-x |
| PII | 10.1007/s10529-020-02933-x |
| PMID | 32519168 |
| MeSH | Bacterial Proteins / genetics Bacterial Proteins / metabolism Cloning, Molecular Flavobacteriaceae / enzymology* Flavobacteriaceae / genetics Gene Expression Glycoside Hydrolases / chemistry Glycoside Hydrolases / genetics* Glycoside Hydrolases / metabolism* Hot Temperature Hydrogen-Ion Concentration Hydrolysis Molecular Weight Protein Sorting Signals Sepharose / chemistry Sequence Analysis, DNA / methods* |
| Resource | |
| General Microbes | JCM32108 |