Characterization of the hydrolysate and catalytic cavity of α-agarase AgaD
| Autor: | Xinzhi Lu, Weibin Zhang, Hua Wang, Zhongxia Lu, Zibo Cui |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
0106 biological sciences
0301 basic medicine Glycoside Hydrolases Stereochemistry Bioengineering Cleavage (embryo) 01 natural sciences Applied Microbiology and Biotechnology Hydrolysate Catalysis 03 medical and health sciences Hydrolysis chemistry.chemical_compound Bacterial Proteins 010608 biotechnology Molecule Binding Sites biology Sepharose Agarase Substrate (chemistry) General Medicine Recombinant Proteins 030104 developmental biology chemistry biology.protein Agarose Gammaproteobacteria Biotechnology |
| Zdroj: | Biotechnology letters. 42(10) |
| ISSN: | 1573-6776 |
| Popis: | To characterize the hydrolysis product and the substrate binding in the catalytic cavity of α-agarase AgaD. The time course curve showed that AgaD degraded agarose by the endo-type cleavage. AgaD did not degrade agarobiose (A2) and agarotetraose (A4). The minimum-length substrate was agarohexaose (A6), which was cleaved into A2 and A4. Agarooctaose (A8) was cleaved into two molecules of A4. Consistently, TLC and NMR data identified agarotetraose (A4) as the main hydrolysate when agarose was degraded by AgaD. This study confirms AgaD is an endo-type α-agarase and A4 as the main hydrolysis product of AgaD, which suggests the catalytic cavity of AgaD accommodates eight sugar units spanning from − 4 to + 4. |
| Databáze: | OpenAIRE |
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