ArticleScientific reports2016
Purification and characterization of a novel phloretin-2'-O-glycosyltransferase favoring phloridzin biosynthesis.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Article
- Dihydrochalcones in Sweet Tea: Biosynthesis, Distribution and Neuroprotection Function.Molecules (Basel, Switzerland) · 2022Review
- Therapeutic Potential and Pharmaceutical Development of a Multitargeted Flavonoid Phloretin.Nutrients · 2022Review
- Metabolic Engineering ofMicroorganisms · 2022Article
- Glycosyltransferases: Mining, engineering and applications in biosynthesis of glycosylated plant natural products.Synthetic and systems biotechnology · 2022Article
- Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach.International journal of molecular sciences · 2019Review
- Characterisation of three novel α-L-arabinofuranosidases from a compost metagenome.BMC biotechnology · 2019Article
- Novel Application of Magnetic Protein: Convenient One-Step Purification and Immobilization of Proteins.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phloretin-2'-O-glycosyltransferase (P2'GT) catalyzes the last glycosylation step in the biosynthesis of phloridzin that contributes to the flavor, color and health benefits of apples and processed apple products. In this work, a novel P2'GT of Malus x domestica (MdP2'GT) with a specific activity of 46.82 μkat/Kg protein toward phloretin and uridine diphosphate glucose (UDPG) at an optimal temperature of 30 °C and pH 8.0 was purified from the engineered Pichia pastoris broth to homogeneity by anion exchange chromatography, His-Trap affinity chromatography and gel filtration. The purified MdP2'GT was low N-glycosylated and secreted as a stable dimer with a molecular mass of 70.7 kDa in its native form. Importantly, MdP2'GT also exhibited activity towards quercetin and adenosine diphosphate glucose (ADPG), kaempferol and UDPG, quercetin and UDP-galactose, isoliquiritigenin and UDPG, and luteolin and UDPG, producing only one isoquercitrin, astragalin, hyperoside, isoliquiritin, or cynaroside, respectively. This broad spectrum of activities make MdP2'GT a promising biocatalyst for the industrial preparation of the corresponding polyphenol glycosides, preferably for their subsequent isolation and purification. Besides, MdP2'GT displayed the lowest K
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