Abstract：
:Hydrolysis of Gracilaria lemaneiformis agar by β-agarase was compared with HCl hydrolysis. The results showed that optimum catalysis conditions for the β-agarase were pH 7.0 at 45°C. Mass spectroscopy, thin-layer chromatography and GPC results showed that the polymerization degrees of the hydrolysis products by the β-agarase were mainly four, six and eight (more specific than the hydrolysate by HCl). The enzymatic degradation products of agar were distinctly different from those of HCl hydrolysis in the ratios among galactose and 3,6-anhydro-galactose and sulfate group contents. The NMR spectrometry proved that the products of β-agarase were neoagaroligosaccharides, which was not found in the agarolytic products by HCl. The neoagarotetraose inhibited tyrosinase activity competitively with the KI value of 16.0mg/ml. Hydroxyl radical-scavenging ability of neoagaroligosaccharides was much greater than that of agar HCl hydrolysate. This work suggests that neoagaroligosaccharide products produced by our β-agarase could be more effective in function than products from acid hydrolysis.
journal_name
Food Chemjournal_title
Food chemistryauthors
Xu XQ,Su BM,Xie JS,Li RK,Yang J,Lin J,Ye XYdoi
10.1016/j.foodchem.2017.07.036subject
Has Abstractpub_date
2018-02-01 00:00:00pages
330-337eissn
0308-8146issn
1873-7072pii
S0308-8146(17)31180-9journal_volume
240pub_type
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