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Characterization of the hydrolysate and catalytic cavity of α-agarase AgaD
Hua Wang1, Weibin Zhang1, Zibo Cui1
1School of Medicine and Pharmacy, Key Laboratory of Marine Drugs, Chinese Ministry of Education, Key Laboratory of Glycoscience & Glycotechnology of Shandong Province, Ocean University of China, Qingdao, 266003, China.
Objective:
To characterize the hydrolysis product and the substrate binding in the catalytic cavity of α-agarase AgaD.
Results:
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.
Conclusion:
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.
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