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Characterization of Thermotolerant Chitinases Encoded by a Brevibacillus laterosporus Strain Isolated from a Suburban Wetland

机译:从郊外湿地分离到的一株嗜热短杆菌菌株编码的耐热几丁质酶的表征。

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To isolate and characterize chitinases that can be applied with practical advantages, 57 isolates of chitin-degrading bacteria were isolated from the soil of a suburban wetland. 16S rRNA gene analysis revealed that the majority of these strains belonged to two genera, Paenibacillus and Brevibacillus. Taking thermostability into account, the chitinases (ChiA and ChiC) of a B. laterosporus strain were studied further. Ni-NTA affinity-purified ChiA and ChiC were optimally active at pH 7.0 and 6.0, respectively, and showed high temperature stability up to 55 °C. Kinetic analysis revealed that ChiC has a lower affinity and stronger catalytic activity toward colloidal chitin than ChiA. With their stability in a broad temperature range, ChiA and ChiC can be utilized for the industrial bioconversion of chitin wastes into biologically active products.
机译:为了分离和表征可以实际应用的几丁质酶,从郊区湿地的土壤中分离了57种分离几丁质的细菌。 16S rRNA基因分析表明,这些菌株大多数属于两个属,即Paenibacillus和Brevibacillus。考虑到热稳定性,进一步研究了B.lateosporus菌株的几丁质酶(ChiA和ChiC)。 Ni-NTA亲和纯化的ChiA和ChiC分别在pH 7.0和6.0时具有最佳活性,并显示了高达55°C的高温稳定性。动力学分析表明,与ChiA相比,ChiC对胶体甲壳素的亲和力更低,催化活性更高。由于ChiA和ChiC在宽广的温度范围内具有稳定性,因此可用于将几丁质废物工业转化为生物活性产品。

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