2001
DOI: 10.1006/prep.2000.1371
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Expression of the Aspergillus aculeatus Endo- β-1,4-mannanase Encoding Gene (man1) in Saccharomyces cerevisiae and Characterization of the Recombinant Enzyme

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Cited by 54 publications
(47 citation statements)
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“…Notwithstanding obstacles such as hyperglycosylation and hindered secretion due to the cell wall, there is an increasing number of examples of effective secretion of heterologous proteins by S. cerevisiae. Native secretion sequences have been found sufficient to effect proper posttranslational processing and secretion of functional proteins in the case of genes originating from fungal sources, including EgI, EgII, and Xyn2 of T. reesei (367,368,521); XynC, XlnA, and Man1 of Aspergillus (129,398,611); and a glucoamylase gene. In-frame fusions to the yeast MF␣1 S secretion sequence have been used to express in S. cerevisiae saccharolytic genes from bacteria, including the end1 gene of B. fibrosolvens, the cel1 gene of R. flavefaciens, the beg1 gene of B. subtilis, and the xlnD gene of A. niger (367,368,701,702,703).…”
Section: Heterologous Cellulase Expression In Bacteriamentioning
confidence: 99%
See 1 more Smart Citation
“…Notwithstanding obstacles such as hyperglycosylation and hindered secretion due to the cell wall, there is an increasing number of examples of effective secretion of heterologous proteins by S. cerevisiae. Native secretion sequences have been found sufficient to effect proper posttranslational processing and secretion of functional proteins in the case of genes originating from fungal sources, including EgI, EgII, and Xyn2 of T. reesei (367,368,521); XynC, XlnA, and Man1 of Aspergillus (129,398,611); and a glucoamylase gene. In-frame fusions to the yeast MF␣1 S secretion sequence have been used to express in S. cerevisiae saccharolytic genes from bacteria, including the end1 gene of B. fibrosolvens, the cel1 gene of R. flavefaciens, the beg1 gene of B. subtilis, and the xlnD gene of A. niger (367,368,701,702,703).…”
Section: Heterologous Cellulase Expression In Bacteriamentioning
confidence: 99%
“…Although these proteins were often extensively glycosylated, they were still efficiently secreted through the yeast cell wall into the medium (367,368). Secretion of a mannanase (Man1) of A. aculeatus was recently reported at levels corresponding to about 5% of cellular protein (611). Looking beyond saccharolytic enzymes, several mutant strains with a "supersecreting" phenotype showing substantially increased secretion of particular proteins have been isolated.…”
Section: Heterologous Cellulase Expression In Bacteriamentioning
confidence: 99%
“…2a,b). With the exception of the -endoglucanase I of T. reesei [31], there was little evidence of overglycosylation (data not shown), which is normally associated with foreign gene expression in S. cerevisiae [40,41].…”
Section: Enzyme Assaysmentioning
confidence: 99%
“…The mannanase is purified and characterized from some types of fungi such as Agaricus bisporus, Aspergillus tamarii, A. aculeatus, A. awamori (Civas et al 1984;Christgau et al 1994;Kurakake and Komaki 2001;Setati et al 2001;Tang et al 2001), from some types of bacteria such as Bacillus agaradhaerens, B. AM001, B. stearothermophilus, B. subtilis, Clostridium thermocellum, Flavobacterium spp., Paenibacillus curdlanolyticus, Dictyoglomus thermophilum (Akino et al 1989;Talbot and Sygusch 1990;Mendoza et al 1994;Zakaria et al 1998;Gibbs et al 1999;Halstead et al 1999;Bettiol and Showell 2002;Pason et al 2006) and from some other organisms such as Lycopersicones culentum (plant), Gastropoda pulmonata (snail), Pomacea insular (snail), Littorina brevicula (mollusk) (Filichkin et al 2009;Charrier and Rouland 2001;Yamamura et al 1996). The microbial β-mannanases are commonly used in improving the quality of food, softening of pulps in paper and pulp industry, reducing the viscosity of coffee extracts, oil extraction and detergent industries (Dhawan and Kaur 2007).…”
Section: Introductionmentioning
confidence: 99%