neoagarotetraose and porphyran

neoagarotetraose has been researched along with porphyran* in 1 studies

Other Studies

1 other study(ies) available for neoagarotetraose and porphyran

ArticleYear
Production of neoagarobiose from agar through a dual-enzyme and two-stage hydrolysis strategy.
    International journal of biological macromolecules, 2020, Oct-01, Volume: 160

    The oligosaccharides from agar hydrolysis have special biological activities, and exhibit application prospects in cosmetic, food and pharmaceutical industry. In this study, two novel β-agarases (AgaA and AgaB) were screened and characterized. It was found that the AgaA was an endo-type agarase which could efficiently hydrolyzed agar or agarose to form neoagarobiose (NA2), neoagarotetraose (NA4) and neoagarohexaose (NA6), while the AgaB was an exo-type and bifunctional enzyme that showed activities towards both agarose and porphyran. Based on the properties of the two enzymes, we developed modular strategy for enzymatic production of neoagarobiose through a two-stage hydrolysis reaction. The cheap substrate agar was first liquefied by AgaA at high temperature to form neoagaroligosaccharides, which together with the sulfated polysaccharides were homogenized by AgaB to form neoagarobiose as the final product. High concentration of agar (10 g/L) was almost completely converted into neoagarobiose with high purity.

    Topics: Agar; Disaccharides; Galactosides; Glycoside Hydrolases; Hydrolysis; Oligosaccharides; Sepharose

2020