Three groups of 15 rats Wistar receive a well-balanced diet with 40 per cent of sucrose (T), lactose (P) or hydrolyzed lactose (PH) in the form of ultrafiltration permeate. After 160 days, no cataract is revealed in the T and P groups. In the PH group, 14 rats reached by cataracts in both eyes: it is slightly developed (PH 2), mildly developed (PH 3) or practically total (PH 4). The inositol disappearance, the high quantity of galactitol, the water and sodium increases are the factors observed before the lens opacification and are responsible for the cataract. Then, during the opacification, soluble proteins, potassium and hydratation of the lens decrease. Galactose 1-P is slowly formed before and during the lens opacification. The lens of the P group (lactose) differ from the control group (T) by the nature and the quantity of hexitols, only.
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JDS Commun
January 2025
Department of Food Science and Technology, The Ohio State University, Columbus, OH 43210.
In this study, a thermostable β-galactosidase from OSU-PECh-4A has been isolated through diafiltration and size-exclusion chromatography. The enzyme consists of a heterodimer with a molecular mass of 110 kDa, with a small and large subunit of 36 and 74 kDa, respectively. The Michaelis constant (K) and maximum velocity (V) values for lactose and -nitrophenyl-β-d-galactopyranoside (NPG) hydrolysis were, respectively, 29.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
The Key Laboratory of Regenerative Biology, Guangzhou Institute of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China.
De novo RNA-sequencing of Wolfiporia cocos mycelia cultured with filter paper composed of cellulose as the sole carbon source revealed a total of five expressed β-glucosidase genes. Among these, the β-glucosidase named Wcbg1B-1, which is composed of 539 amino acid residues and belongs to the GH1 family, had the highest mRNA abundance, accounting for 65 % of the total mRNA of the five expressed β-glucosidases. The recombinant Wcbg1B-1 was successfully expressed in Escherichia coli, with an optimal pH of 6.
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.
View Article and Find Full Text PDFJ Biotechnol
February 2025
State Key Laboratory of Marine Food Processing and Safety Control, College of Food Science and Engineering, Ocean University of China, Qingdao 266404, PR China; Qingdao Key Laboratory of Food Biotechnology, Qingdao 266404, PR China; Key Laboratory of Biological Processing of Aquatic Products, China National Light Industry, Qingdao 266404, PR China. Electronic address:
Surface display technology has garnered significant attention for preparing efficient whole cell catalysts, while reported carrier proteins still cannot meet the demand to display various passenger domains, especially for those with high molecular weight. This study demonstrates that the autotransporter of esterase Est7 (E7AT) from Stenotrophomonas maltophilia played a decisive role in its efficient surface display. Guided by the original signal peptide, the surface display ratio of Est7 was determined as 89.
View Article and Find Full Text PDFInt J Food Microbiol
February 2025
College of Life Science, Shandong Normal University, Jinan 250358, China. Electronic address:
β-Galactosidases can be used to degrade lactose in milk to prepare lactose-free milk, which is sweeter than ordinary milk and suitable for people with lactose intolerance. The β-galactosidase gene (WcGal2809) was cloned from Weissella confusa SW1 and successfully expressed in Escherichia coli BL21(DE3). The active WcGal2809 was identified to be a heterodimer composed of two distinct proteins LacL (72.
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