Regular ArticleExtensive N-Glycosylation Reduces the Thermal Stability of a Recombinant Alkalophilic Bacillus α-Amylase Produced in Pichia pastoris
References (36)
- et al.
Amino acid residues stabilizing a Bacillus α-amylase against irreversible thermoinactivation
J. Biol. Chem.
(1989) - et al.
Subsite mapping of enzymes: Correlation of product patterns with Michaelis parameters and substrate induced strain
J. Biol. Chem.
(1971) - et al.
Action patterns of various exo-amylases and the anomeric configurations of their products
Carbohydr. Res.
(1984) - et al.
Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution
J. Mol. Biol.
(1995) - et al.
Activation of Bacillus licheniformis α-amylase through a disorder → order transition of the substrate-binding site mediated by a calcium–sodium–calcium metal triad
Structure
(1998) Advances in the use of Pichia pastoris for high-level gene expression
Curr. Opin. Biotechnol.
(1995)- et al.
Overexpression, purification, and characterization of recombinant barley α-amylases 1 and 2 secreted by the methylotrophic yeast Pichia pastoris
Protein Express. Purif.
(1996) - et al.
Variation in N-linked oligosaccharide structures in heterologous proteins secreted by the methylotrophic yeast Pichia pastoris
Protein Expr. Purif.
(1998) - et al.
Improved activity and modulated action pattern obtained by random mutagenesis at the fourth β-α loop involved in substrate binding to the catalytic (β/α)8-barrel domain of barley α-amylase 1
J. Biol. Chem.
(1997) - et al.
Expression of cDNAs encoding barley α-amylase 1 and 2 in yeast and characterization of the secreted proteins
Gene
(1990)
Overview of N- and O-linked oligosaccharide structures found in various yeast species
Biochim. Biophys. Acta
The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency
J. Biol. Chem.
Why is one Bacillus α-amylase more resistant against irreversible thermal inactivation than another?
J. Biol. Chem.
C-terminal truncations of a thermostable Bacillus stearothermophilus α-amylase
Protein Eng.
Hybrid Bacillus amyloliquefaciens × Bacillus licheniformis α-amylases: Construction, properties and sequence determinants
Eur. J. Biochem.
Hyperthermostable mutants of Bacillus licheniformis α-amylase: Multiple amino acid replacements and molecular modelling
Protein Eng.
Hyperthermostable mutants of Bacillus licheniformis α-amylase: Thermodynamic studies and structural interpretation
Protein Eng.
Cited by (32)
Characteristics of a recombinant Lentinula edodes endoglucanase and its potential for application in silage of rape straw
2019, International Journal of Biological MacromoleculesCitation Excerpt :These results were slight different from the report by Takeda et al. (2013) [16], in which the LeCel12A activity was maximum at 40 °C and pH 4.5. Different expression system used and the presence or absence of native signal peptide [27] and glycosylation [28] may be responsible for these discrepancy. The LeCel12A activity was enhanced by 10.5%, 14.1%, and 31.6% in the presence of 5 mM of KCl, ZnCl2, and MnCl2, respectively, but was reduced by other salts, especially CuCl2 (Fig. 3c).
Expression and characterization of Bacillus subtilis PY22 α-amylase in Pichia pastoris
2010, Journal of Molecular Catalysis B: EnzymaticThe influence of N-glycosylation on biochemical properties of Amy1, an α-amylase from the yeast Cryptococcus flavus
2009, Carbohydrate ResearchCitation Excerpt :The native enzyme treated at 50 °C for 60 min retained 97.8% of its maximum activity, whereas the activity of the non-glycosylated form under the same conditions was lowered to about 94.5% (Table 3). The difference in the behavior of the enzyme in terms of activity and stability after the addition of tunicamycin during synthesis may be due to the decreased carbohydrate content, as previously reported in the literature.2,19,20 These results suggest that the function of the N-linked carbohydrate may be to stabilize the structure of the α-amylase produced by C. flavus and so protect it from physical and proteolytic attack after secretion.
Expression of a Bacillus subtilis pectate lyase gene in Pichia pastoris
2008, Biochemical Engineering JournalExpression of the human activin type I and II receptor extracellular domains in Pichia pastoris
2006, Protein Expression and Purification
- 1
Permanent address: The Walter and Eliza Hall Institute of Medical Research, Post Office, The Royal Melbourne Hospital, Victoria 3050, Australia.
- 2
Permanent address: M & E Biotech A/S, Kogle Allé 6, DK-2970 Hørsholm, Denmark.
- 3
To whom correspondence and reprint requests should be addressed. Fax: +45 33 27 47 08. E-mail: [email protected].