This study investigated the impact of a transglycosylated product (ACOD) catalyzed by MKSR dextransucrase using sucrose as a glucosyl donor and both maltose and as acceptors on gut microbiota through fecal fermentation. ACOD promoted the growth of probiotics such as , , GG, and MKSR, while inhibiting the growth of pathogenic bacteria such as , O157:H7, , , , , , , and during independent cultivation. Fecal fermentation for 24 h revealed that ACOD significantly increased the production of short-chain fatty acids (SCFAs) compared to the blank and fructoooligosaccharide (FOS) groups. Specifically, ACOD led to a 4.5-fold increase in acetic acid production compared to FOSs and a 3.3-fold increase in propionic acid production. Both the ACOD and FOS groups exhibited higher levels of butyric acid than the blank. Notably, ACOD significantly modulated the composition of the gut microbiota by increasing the relative abundances of and decreasing and In contrast, FOSs remarkably promoted the growth of . These findings suggest that ACOD is a potential candidate for prebiotics that improve the intestinal environment by being actively used by beneficial bacteria.
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http://dx.doi.org/10.3390/foods13203267 | DOI Listing |
Biotechnol Biofuels Bioprod
January 2025
College of Life Sciences, Henan Agricultural University, 218 Ping-an Ave., Zhengzhou, 450046, China.
Background: Aspergillus niger is an important lignocellulose-degrading enzyme-producing strain. Multiple regulatory factors regulate the synthesis of lignocellulose-degrading enzymes in A. niger.
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January 2025
Department of Biochemistry, Phramongkutklao College of Medicine, Phramongkutklao Hospital, Bangkok 10400, Thailand. Electronic address:
In this study, maltotriosyl-erythritol (EG) was synthesized as a novel prebiotic candidate via transglycosylation using recombinant amylomaltase (AMase) from Thermus sp. Tapioca starch served as the glucosyl donor, and erythritol as the acceptor. High-performance liquid chromatography (HPLC) revealed an EG yield of 14.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Department of Pharmaceutical Technology and Biochemistry, Faculty of Chemistry, Gdansk University of Technology, Narutowicza 11/12, 80-233 Gdansk, Poland.
Cold-adapted microorganisms possess cold-active enzymes with potential applications in different industries and research areas. In this study, two genes encoding β-d-galactosidases belonging to Glycoside Hydrolase families 2 and 42 from the psychrotolerant Arctic bacterium sp. S3* were cloned, expressed in and , purified and characterized.
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December 2024
Faculty of Food Science and Engineering, Kunming University of Science and Technology, Kunming, Yunnan 650500, China. Electronic address:
The recombinated amylopullulanase of PulW310B, pullulanase from Bacillus aryabhattai W310, was characterized. Sequence analysis of PulW310B showed that PulW310B has type I pullulanase structures including its typical region and the conserved regions of glycoside hydrolase family 13. Moreover, PulW310B was predicted to has typical domains of pullulanase and SSF51445 belonging to tansglycosidase.
View Article and Find Full Text PDFInt J Biol Macromol
February 2025
Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, Changchun 130012, China. Electronic address:
Enzymatic glycosylation is an efficient and biocompatible approach to enhance natural product bioavailability. Cellobiose phosphorylase, a novel glycosyltransferase, utilizes 1-phospho-glucose (1-p-Glc) as a glycosyl donor for regioselective glycosylation of various natural substrates. However, the high cost of 1-p-Glc limits the economic feasibility of the process.
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