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Title 

Properties of a glycogen like polysaccharide produced by a mutant of Escherichia coli lacking glycogen synthase and maltodextrin phosphorylase

Authors 

J Y KwakM G KimY W KimHyun Seung BanMi Sun WonJ T ParkK H Park

Publisher 

Elsevier

Issue Date 

2016

Citation 

Carbohydrate Polymers, vol. 136, no. 0, pp. 649-655

Keywords 

AmylaseDigestibility kineticsEscherichia coli mutantGlycogenImmunostimulating effectIntracellular polysaccharideWater solubility

Abstract 

Escherichia coli mutant TBP38 lacks glycogen synthase (GlgA) and maltodextrin phosphorylase (MalP). When grown on maltose in fed-batch fermentation TBP38 accumulated more than 50-fold higher glycogen-type polysaccharide than its parental strain. The polysaccharides were extracted at different growth stages and migrated as one peak in size-exclusion chromatography. TBP38 produced polysaccharides ranging 2.6 × 106-4.6 × 106 Da. A ratio of short side-chains (DP 12) in the polysaccharides was greater than 50%, and number-average degree of polymerization varied from 9.8 to 8.4. The polysaccharides showed 70-290 times greater water-solubility than amylopectin. Km values using porcine and human pancreatic α-amylases with polysaccharides were 2- to 4-fold larger than that of amylopectin. kcat values were similar for both α-amylases. The TBP38 polysaccharides had 40-60% lower digestibility to amyloglucosidase than amylopectin. Intriguingly, the polysaccharides showed strong immunostimulating effects on mouse macrophage cell comparable to lipopolysaccharides. The lipopolysaccharide contamination levels were too low to account for this effect.

ISSN 

0144-8617

Link 

http://dx.doi.org/10.1016/j.carbpol.2015.09.091

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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