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Modification of the Loop Region Near the Substrate Tunnel to Alter the Hydrolytic Process of Dextranase.
- Source :
-
Journal of Biotechnology . Feb2024, Vol. 381, p57-66. 10p. - Publication Year :
- 2024
-
Abstract
- Dextranases are hydrolases that exclusively catalyze the disruption of α−1,6 glycosidic bonds. A series of variant enzymes were obtained by comparing the sequences of dextranases from different sources and introducing sequence substitutions. A correlation was found between the number of amino acids in the 397–401 region and the hydrolytic process. When there were no more than 5 amino acids in the 397–401 region, the enzyme first hydrolyzed the dextran T70 to a low molecular weight dextran with a molecular weight of about 5000, then IMOs 1 1 IMOs: isomaltooligosaccharides. G: glucose, G2: maltose, G3: maltotriose, G4: maltotetraose, G5: maltopentaose, G6: maltohexaose, G7: maltoheptaose, IG2: isomaltose, IG3: isomaltotriose, IG4: isomaltotetraose, IG5: isomaltopentaose appeared in the system if the degradation continued, showing a clear sequential relationship. And when there are more than 5 amino acids in the 397–401 region, IMOs were produced at the beginning of hydrolysis and continue to increase throughout the hydrolytic process. At the same time, we investigated the enzymatic properties of the variants and found that the hydrolytic rate of A-Ca was 11 times higher than that of the original enzyme. The proportion of IMOs produced by A-Ca was 80.68%, which was nearly10% higher than the original enzyme, providing a new enzyme for the industrial preparation of IMOs. • One of the factors affecting the hydrolysis process of Aodex was determined. • Using sequence substitution method for molecular modification. • The hydrolysis rate of variant A-Ca increased by 11 times. • The proportion of IMOs produced by A-Ca was 80.68% which increased by nearly 10% compared to the WT. [ABSTRACT FROM AUTHOR]
- Subjects :
- *MOLECULAR weights
*MALTOSE
*DEXTRAN
*AMINO acids
*HYDROLASES
Subjects
Details
- Language :
- English
- ISSN :
- 01681656
- Volume :
- 381
- Database :
- Academic Search Index
- Journal :
- Journal of Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 175164563
- Full Text :
- https://doi.org/10.1016/j.jbiotec.2024.01.003