Partial purification and chemical characterization of a glycoprotein (putative hydrocolloid) emulsifier produced by a marine bacterium Antarctobacter

During screening for novel emulsifiers and surfactants, a marine alphaproteobacterium, Antarctobacter sp. TG22, was isolated and selected for its production of an extracellular emulsifying agent, AE22. This emulsifier was produced optimally in a low-nutrient seawater medium supplemented with glucose...

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Bibliographic Details
Published in:Applied Microbiology and Biotechnology
Main Authors: Gutierrez, Tony, Mulloy, Barbara, Bavington, Charles, Black, Kenny, Green, David
Format: Article in Journal/Newspaper
Language:English
Published: 2007
Subjects:
Online Access:https://pure.uhi.ac.uk/en/publications/b3cb75ec-0d86-4f1e-9eed-1afb987862e9
https://doi.org/10.1007/s00253-007-1091-9
Description
Summary:During screening for novel emulsifiers and surfactants, a marine alphaproteobacterium, Antarctobacter sp. TG22, was isolated and selected for its production of an extracellular emulsifying agent, AE22. This emulsifier was produced optimally in a low-nutrient seawater medium supplemented with glucose and was extractable by cold ethanol precipitation of the high-molecular-weight fraction (> 100 kDa). Production of AE22 commenced towards the late exponential phase of growth, with maximum emulsifying activity detected after approximately 4 days of the cells entering the death phase. Chemical, chromatographic and nuclear magnetic resonance spectroscopic analysis confirmed AE22 to be a high-molecular-weight (> 2,000 kDa) glycoprotein with high uronic acids content, thus denoting an apparent polyanionic structure. Functional characterization showed this polymer to compare well to xanthan gum and gum arabic as an emulsion-stabilizing agent for a range of different food oils. However, AE22 exhibited better stabilizing than emulsifying properties, which could be conferred by its viscosifying effect in solution or from certain chemical groups found on the polysaccharide or protein moieties of the polymer. This new high-molecular-weight glycoprotein exhibits interesting functional qualities that are comparable to other biopolymers of this type and shows particular promise as an emulsion-stabilizing agent in biotechnological applications.