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Profil bibliographique

Motomitsu Kitaoka

Informations fournies par OpenAlex. Research Africa ne déduit ni nationalité, ni poste, ni coordonnées personnelles.

283Publications signalées
8813Citations signalées
1Affiliations récentes

Les institutions déclarées

Les domaines associés

Enzyme Production and CharacterizationMicrobial Metabolites in Food BiotechnologyCarbohydrate Chemistry and SynthesisBiofuel production and bioconversionEnzyme Catalysis and Immobilization

Les publications récentes

Accès ouvert 2026 preprint OpenAlex

Crystal structure of a class II UDP-glucose–hexose-1-phosphate uridylyltransferase from Bifidobacterium longum involved in human milk oligosaccharide metabolism

Mayo Sato, Chihaya Yamada, Mamoru Nishimoto, Motomitsu Kitaoka et autres

Infant-associated bifidobacteria utilize lacto- N -biose I (LNB) and galacto- N -biose (GNB), major components of human milk oligosaccharides and intestinal mucin, respectively, through the GNB/LNB metabolic pathway. A UDP-glucose–hexose-1-phosphate uridylyltransferase (GalT) from Bifidobacterium longum JCM 1217 (BlGalT2) catalyzes a key step …

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0 citations bioRxiv (Cold Spring Harbor Laboratory)
2026 article OpenAlex

Lacto- N -biose Improves Acute Colitis in Mice by Modulating Gut Microbiota and Metabolites

Zixin Fan, Wanying Xie, Xiaopei Hu, Li Y et autres

Abstract Lacto-N-biose (LNB) as the core structure among human milk oligosaccharides remained insufficiently characterized in terms of the potential to ameliorate colitis. This study investigated effects of LNB in colitis by using dextran sulfate sodium salt to induce mouse model. Results demonstrated …

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1 citation Journal of Agricultural and Food Chemistry
2026 article OpenAlex

One-pot synthesis of lacto- N -tetraose using a glycosynthase engineered from GH136 lacto- N -biosidase LnbX

Noriki Fujio, Ryota Umekage, Ami Ishikawa, Yuji Honda et autres

Lacto-N-tetraose (LNT: Galβ1-3GlcNAcβ1-3Galβ1-4Glc) is the most abundant core structure of human milk oligosaccharides (HMOs) and plays important roles in establishing healthy microbiota in the infant gut. Several enzymatic strategies have been developed for the synthesis of LNT. In the conventional linear approach, …

jp (code pays fourni par la source)

0 citations Glycobiology
Accès ouvert 2024 article OpenAlex

Efficient Synthesis of β-Glucose 1-Phosphate through Enzymatic Phosphorolysis and Baker's Yeast Fermentation

Sofia Koltovskaia, Akane Ohtao, Motomitsu Kitaoka, Hiroyuki Nakai et autres

β-Glucose 1-phosphate (βGlc1P) is a donor substrate in the synthesis of various α-glucosides by glycoside phosphorylases belonging to the glycoside hydrolase family 65. This study presents an efficient synthesis of βGlc1P combining enzymatic phosphorolysis of inexpensive maltose and baker's yeast fermentation to …

jp (code pays fourni par la source)

0 citations Journal of Applied Glycoscience
Accès ouvert 2024 article OpenAlex

Molecular Basis of Absorption at 340 nm of 3-Ketoglucosides under Alkaline Conditions

Motomitsu Kitaoka, A. Takano, Mei Takahashi, Yoshiki Yamakawa et autres

Transient absorption at 340 nm under alkaline conditions has long been used to detect the presence of 3-keto-O-glycosides without understanding the molecular basis of the absorbance. The time course of A340 nm for the alkaline treatment of 3-ketolevoglucosan, an intramolecular 3-keto-O-glycoside, was …

jp (code pays fourni par la source)

0 citations Journal of Applied Glycoscience
Accès ouvert 2023 article OpenAlex

Encapsulation of Lacto‐N‐biose based on ovalbumin and carboxymethyl cellulose microparticles: fabrication, characterisation and thermal stability

Xin Huang, Yue Sun, Suhong Li, Motomitsu Kitaoka et autres

Summary To improve the thermal stability Lacto‐N‐biose (LNB), it was encapsulated by the OVA‐CMC microparticles system. When the mass ratio of OVA:CMC:LNB was 1.5:1:1, the particle size of microparticles was 623 ± 4 nm, and the encapsulation efficiency and loading efficiency of …

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2 citations International Journal of Food Science & Technology
Accès ouvert 2023 article OpenAlex

Substrate recognition mode of a glycoside hydrolase family 42 β-galactosidase from Bifidobacterium longum subspecies infantis(BiBga42A) revealed by crystallographic and mutational analyses

Aina Gotoh, Masafumi Hidaka, Haruko Sakurama, Mamoru Nishimoto et autres

Aim:Bifidobacterium longum subsp. infantis uses a glycoside hydrolase (GH) family 42 β-galactosidase (BiBga42A) for hydrolyzing lacto-N-tetraose (LNT), which is the most abundant core structure of human milk oligosaccharides (HMOs). As such, BiBga42A represents one of the pivotal enzymes underpinning the symbiosis between …

jp (code pays fourni par la source)

9 citations Microbiome Research Reports
Accès ouvert 2022 article OpenAlex

Automatic Calculation of the Kinetic Parameters of Enzymatic Reactions with Their Standard Errors Using Microsoft Excel

Motomitsu Kitaoka

We created a Microsoft Excel file, Enzyme_Kinetics_Calculator, which includes macro programs that automatically calculates kinetic parameters for typical kinetic equations of enzymatic reactions, accompanied by their standard errors, by minimizing the residual sum of squares thereof. The [S]-v plot is automatically drawn …

jp (code pays fourni par la source)

31 citations Journal of Applied Glycoscience
Accès ouvert 2022 article OpenAlex

Priority effects shape the structure of infant-type Bifidobacterium communities on human milk oligosaccharides

Miriam N. Ojima, Lin Jiang, Aleksandr A. Arzamasov, Keisuke Yoshida et autres

Bifidobacteria are among the first colonizers of the infant gut, and human milk oligosaccharides (HMOs) in breastmilk are instrumental for the formation of a bifidobacteria-rich microbiota. However, little is known about the assembly of bifidobacterial communities. Here, by applying assembly theory to …

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122 citations The ISME Journal

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