An Atomic Force Microscopy Study on the Effect of β-Galactosidase, α-L-Rhamnosidase and α-L-Arabinofuranosidase on the Structure of Pectin Extracted from Apple Fruit Using Sodium Carbonate

The enzyme driven changes in plant cell wall structure during fruit ripening result in debranching, depolymerization and solubilization of pectin polysaccharides, which has an effect in terms of the postharvest quality losses in fruit. Atomic force microscopy (AFM) has revealed that diluted alkali s...

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Bibliographic Details
Main Authors: Piotr Mariusz Pieczywek, Justyna Cybulska, Artur Zdunek
Format: Article
Language:English
Published: MDPI AG 2020-06-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:https://www.mdpi.com/1422-0067/21/11/4064
Description
Summary:The enzyme driven changes in plant cell wall structure during fruit ripening result in debranching, depolymerization and solubilization of pectin polysaccharides, which has an effect in terms of the postharvest quality losses in fruit. Atomic force microscopy (AFM) has revealed that diluted alkali soluble pectins (DASP) from fruit and vegetables have an interesting tendency to self-assemble into regular structures. However, the mechanism is not yet fully understood. The current study is aimed at investigating the role of neutral sugars, namely galactose, rhamnose and arabinose in the formation of the branched structure of DASP. β-galactosidase, α-L-rhamnosidase and α-L-arabinofuranosidase enzymes were used for the treatment of DASP extracted from Golden Delicious apple flesh (<i>Malus domestica</i> cv. Golden Delicious). The effects of the selective degradation of pectic polysaccharides after 15, 30, 60, 90 and 120 min of incubation were observed using AFM. The α-L-rhamnosidase enzyme activity on pectin extracted with Na<sub>2</sub>CO<sub>3</sub> did not cause any visible or measurable degradation of the molecular structure. The moderate effects of β-galactosidase enzymatic treatment suggested the possible role of galactose in the branching of DASP molecules deposited on mica. Data obtained for α-L-arabinofuranosidase indicated the crucial role of arabinose in the formation and preservation of the highly branched structure of the DASP fraction.
ISSN:1661-6596
1422-0067