Novel α-1,3/α-1,4-Glucosidase from Aspergillus niger Exhibits Unique Transglucosylation to Generate High Levels of Nigerose and Kojibiose
| Autor: | Asako Kikuchi, Min Ma, Patcharapa Klahan, Masayuki Okuyama, Atsuo Kimura, Takayoshi Tagami |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0106 biological sciences
Kojibiose Glycosylation Mutant Nigerose Disaccharides 01 natural sciences Pichia pastoris Substrate Specificity Fungal Proteins chemistry.chemical_compound Maltotriose chemistry.chemical_classification biology Hydrolysis 010401 analytical chemistry Aspergillus niger alpha-Glucosidases General Chemistry Maltose biology.organism_classification 0104 chemical sciences Enzyme Biochemistry chemistry Biocatalysis General Agricultural and Biological Sciences 010606 plant biology & botany |
| Zdroj: | Journal of agricultural and food chemistry. 67(12) |
| ISSN: | 1520-5118 |
| Popis: | α-Glucosidase from Aspergillus niger (AgdA; typical α-1,4-glucosidase) is known to industrially produce α-(1→6)-glucooligosaccharides. This fungus also has another α-glucosidase-like protein, AgdB. To learn its function, wild-type AgdB was expressed in Pichia pastoris. However, the enzyme displayed two electrophoretic forms due to heterogeneity of N-glycosylation at Asn354. The deglycosylation mutant N354D shared the same properties with wild-type AgdB. N354D demonstrated hydrolytic specificity toward α-(1→3)- and α-(1→4)-glucosidic linkages, indicating that AgdB is an α-1,3-/α-1,4-glucosidase. N354D-catalyzed transglucosylation from maltose was analyzed in short- and long-term reactions, enabling us to learn the transglucosylation specificity and product accumulation, respectively. A short-term reaction ( |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|