@article{mbs:/content/journal/micro/10.1099/00221287-137-3-579, author = "Olsen, Ole and Thomsen, Karl Kristian", title = "Improvement of bacterial β-glucanase thermostability by glycosylation", journal= "Microbiology", year = "1991", volume = "137", number = "3", pages = "579-585", doi = "https://doi.org/10.1099/00221287-137-3-579", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-137-3-579", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "The relationship between enzyme stability and glycosylation was examined for two different Bacillus (1,3-1,4)-β-glucanases following expression of the corresponding genes in Escherichia coli and in Saccharomyces cerevisiae. Both of the (1,3-1,4)-β-glucanases secreted from yeast cells were glycosylated and a pronounced difference in the type and extent of glycosylation was observed. Thermostability analysis of the glycosylated enzymes and their unglycosylated counterparts synthesized by E. coli disclosed a substantially higher thermotolerance of the glycosylated enzymes. At 70 °C the half-life of the glycosylated form of B. macerans (1,3-1,4)-β-glucanase was 26 min, as compared to 10 min for the unglycosylated form of the enzyme. Using the same conditions, the half-life of the B. amyloliquefaciens-B. macerans hybrid (1,3-1,4)-β-glucanase was 5 min for the unglycosylated enzyme and about 100 min when the enzyme was glycosylated.", }