ArticlePloS one2015
Catalytic efficiency of chitinase-D on insoluble chitinous substrates was improved by fusing auxiliary domains.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Engineering fusion enzymes for enhanced catalysis and stability: strategies and biotechnological applications.Molecular biology reports · 2026Review
- The Impact of Chitinase Binding Domain Truncation on the Properties ofMarine drugs · 2025Article
- Exploring the Structural and Dynamic Properties of a Chimeric Glycoside Hydrolase Protein in the Presence of Calcium Ions.International journal of molecular sciences · 2024Article
- Multidomain chimeric enzymes as a promising alternative for biocatalysts improvement: a minireview.Molecular biology reports · 2024Review
- Enhancing the endo-activity of the thermophilic chitinase to yield chitooligosaccharides with high degrees of polymerization.Bioresources and bioprocessing · 2024Article
- Formation of recombinant bifunctional fusion protein: A newer approach to combine the activities of two enzymes in a single protein.PloS one · 2022Article
- Two Highly Similar Chitinases from MarineMarine drugs · 2020Article
- Chitinase: diversity, limitations, and trends in engineering for suitable applications.Bioscience reports · 2018Review
- Cloning, purification, and characterization of an organic solvent-tolerant chitinase, MtCh509, fromBiotechnology for biofuels · 2018Article
- Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical analyses.Scientific reports · 2015Article
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Authors and funding
4 authors.
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Abstract
Chitin is an abundant renewable polysaccharide, next only to cellulose. Chitinases are important for effective utilization of this biopolymer. Chitinase D from Serratia proteamaculans (SpChiD) is a single domain chitinase with both hydrolytic and transglycosylation (TG) activities. SpChiD had less of hydrolytic activity on insoluble polymeric chitin substrates due to the absence of auxiliary binding domains. We improved catalytic efficiency of SpChiD in degradation of insoluble chitin substrates by fusing with auxiliary domains like polycystic kidney disease (PKD) domain and chitin binding protein 21 (CBP21). Of the six different SpChiD fusion chimeras, two C-terminal fusions viz. ChiD+PKD and ChiD+CBP resulted in improved hydrolytic activity on α- and β-chitin, respectively. Time-course degradation of colloidal chitin also confirmed that these two C-terminal SpChiD fusion chimeras were more active than other chimeras. More TG products were produced for a longer duration by the fusion chimeras ChiD+PKD and PKD+ChiD+CBP.
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