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Start Over Author "Liyuan Dai" Publisher elsevier bv
5 results on '"Liyuan Dai"'

5. A cold-active 1,4-α-glucan branching enzyme from Bifidobacterium longum reduces the retrogradation and enhances the slow digestibility of wheat starch

Author

Xuexia Fu, Teng Fei, Xiaolei Li, Liyuan Dai, Yong Wang, Dan Li, and Yakun Zhao

Subjects
Bifidobacterium longum, Retrogradation (starch), Amylopectin, medicine.disease_cause, Analytical Chemistry, chemistry.chemical_compound, Amylose, 1,4-alpha-Glucan Branching Enzyme, Escherichia coli, Glycogen branching enzyme, medicine, Amino Acid Sequence, Food science, Phylogeny, Triticum, Glucan, chemistry.chemical_classification, biology, Temperature, food and beverages, Substrate (chemistry), Starch, General Medicine, Hydrogen-Ion Concentration, biology.organism_classification, Molecular Weight, chemistry, biology.protein, Thermodynamics, Sequence Alignment, Food Science
Abstract

To develop a 1,4-α-glucan branching enzyme (BE) without homology to known allergens, the glgB gene from Bifidobacterium longum was overexpressed under the control of BLMA promoter in Escherichia coli. B. longum BE (BlBE) had a molecular weight of 86.1 kDa and a specific activity of more than 18.5 U/mg protein at 25–35 °C and pH 5.5–7.0, and exhibited 30% of the maximum activity at 10 °C. The cold-active BlBE preferred to transfer maltohexaose and introduced DP 4–36 branches into amylose. BlBE also increased the proportion of DP 2–10 branches in amylopectin and decreased its Mw from 1.39 × 106 to 1.16 × 105 g/mol. As the BlBE concentration increased from 0.0 to 0.5 U/mg substrate, the retrogradation enthalpy of BlBE-modified wheat starch decreased from 4.50 to 1.83 J/g (p

Published
2020
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