AI Article Synopsis
- The genome of Kitasatospora setae KM-6054 contains three chitosanase genes (csn1-3) that were cloned and expressed in Streptomyces lividans, resulting in the purification of four chitosanase enzymes.
- The study found that the csn2 gene produces two distinct proteins, while Csn1 and Csn2H are typical GH46 chitosanases, and Csn3 is more similar to bacilli chitosanases.
- The enzymes demonstrated various activities under different conditions, revealing significant biochemical diversity, and the findings provide insights into their structural characteristics through 3D modeling and sequence comparisons.
Article Abstract
The genome of Kitasatospora setae KM-6054, a soil actinomycete, has three genes encoding chitosanases belonging to GH46 family. The genes (csn1-3) were cloned in Streptomyces lividans and the corresponding enzymes were purified from the recombinant cultures. The csn2 clone yielded two proteins (Csn2BH and Csn2H) differing by the presence of a carbohydrate-binding domain. Sequence analysis showed that Csn1 and Csn2H were canonical GH46 chitosanases, while Csn3 resembled chitosanases from bacilli. The activity of the four chitosanases was tested in a variety of conditions and on diverse chitosan forms, including highly N-deacetylated chitosan or chitosan complexed with humic or polyphosphoric acid. Kinetic parameters were also determined. These tests unveiled the biochemical diversity among these chitosanases and the peculiarity of Csn3 compared with the other three enzymes. The observed biochemical diversity is discussed based on structural 3D models and sequence alignment. This is a first study of all the GH46 chitosanases produced by a single microbial strain.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5635096 | PMC |
| http://dx.doi.org/10.1007/s00253-017-8517-9 | DOI Listing |
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