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http://dx.doi.org/10.1002/jps.3030380402 | DOI Listing |
Curr Pharm Des
January 2025
Department of Pharmaceutics, PSG College of Pharmacy, Coimbatore 600 004, Tamil Nadu, India.
Introduction: The objective of the present study was to improve the anti-inflammatory and antibacterial activities of mastic gum resin (MGR). MGR was loaded into a phospholipid nanocarrier with or without partially hydrolyzed ginsenoside, followed by dispersion into distilled water.
Method: The phospholipid nanocarrier dispersion showed significantly enhanced in-vitro release, porcine skin/ intestine permeation, and retention.
Klin Padiatr
January 2025
Department Of Pediatrics, Division of Pneumology, Allergology, Infectious Diseases and Gastroenterology, Goethe University Frankfurt, Frankfurt am Main, Germany.
Premastication is a traditional feeding method whereby solids are pre-chewed by the mother or sometimes by other relatives and then given to the infant along with the oral microbiota. The aim of this study was to assess if premastication is known or performed among the German population as well as to evaluate the expectations regarding this feeding method, particularly in the context of allergy prevention. Two surveys about premastication were conducted.
View Article and Find Full Text PDFAppl Biochem Biotechnol
January 2025
Unidad de Biotecnología Industrial, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C, 45019, Zapopan, Jal, Mexico.
Lipases from the basidiomycete fungus Ustilago maydis are promising but underexplored biocatalysts due to their high homology with Candida antarctica lipases. This study provides a comprehensive characterization of a recombinant CALB-like lipase from U. maydis, expressed in Pichia pastoris (rUMLB), and compares its properties with those of the well-studied recombinant lipase B from C.
View Article and Find Full Text PDFMolecules
December 2024
State Key Laboratory of Oil and Gas Reservoir Geology and Exploitation, Southwest Petroleum University, Chengdu 610500, China.
Int Immunopharmacol
February 2025
AT-31 BIO Inc., 403 Business Incubation Center, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Republic of Korea; Laboratory of Immunobiology, School of Life Science and Biotechnology, College of Natural Sciences, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Republic of Korea. Electronic address:
Recombinant GH16B β-agarase-catalyzed liquefaction of 5-7 %(w/v) melted agarose at 50 °C completely hydrolyzed agarose into neoagarohexaose (NA6) and neoagarotetraose (NA4). Subsequent saccharification by recombinant GH50A β-agarase or recombinant GH50A β-agarase/recombinant GH117A α-neoagarobiose hydrolase at 35 °C converted NA6/NA4 into neoagarobiose (NA2) or 3,6-anhydro-L-galactose (L-AHG)/D-galactose, respectively. Purification of NA6/NA4 and NA2 was achieved by Sephadex G-15 column chromatography, while L-AHG was purified by Sephadex G-10, achieving ≥ 98 % purity.
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