Characterization of the hydrolysate and catalytic cavity of α-agarase AgaD.

Abstract:

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.

journal_name

Biotechnol Lett

journal_title

Biotechnology letters

authors

Wang H,Zhang W,Cui Z,Lu Z,Lu X

doi

10.1007/s10529-020-02901-5

subject

Has Abstract

pub_date

2020-10-01 00:00:00

pages

1919-1925

issue

10

eissn

0141-5492

issn

1573-6776

pii

10.1007/s10529-020-02901-5

journal_volume

42

pub_type

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