Abstract：
:Enzymatic curdlan hydrolysis is gaining more attention for the value of oligo-β-glucans in many aspects. Currently, the triple-helical conformation of curdlan fiber was imposed to the structure of β-1,3-glucanase as its substrate without experimental evidence. Here, solution conformation of differently treated curdlan and each hydrolysis rate by a variety of β-1,3-glucanases were systematically examined. Results showed that different enzymes exhibited preferences over the trajectories of pH change that curdlan solution went through, and all enzymes hydrolyzed heat treated curdlan solution at their maximum rates where most of the higher ordered helices were diminished. Combined with molecular docking studies, a multi-step hydrolysis process was proposed. Recognition of triple-helical curdlan by their ancillary region of β-1,3-glucanase occurred before its unwinding into single- and double-helical forms, and the later ones fitted better to the catalytic cavity of the enzyme where the polysaccharides chain eventually got hydrolyzed into oligo-β-glucans.
journal_name
Food Chemjournal_title
Food chemistryauthors
Yu P,Zhou F,Yang Ddoi
10.1016/j.foodchem.2019.02.070subject
Has Abstractpub_date
2019-07-30 00:00:00pages
20-27eissn
0308-8146issn
1873-7072pii
S0308-8146(19)30393-0journal_volume
287pub_type
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