| Literature DB >> 31100392 |
Saumya Singh1, Gursharan Singh2, Madhu Khatri1, Anupreet Kaur1, Shailendra Kumar Arya3.
Abstract
The present work aims to characterize thermo and alkali stable β-mannanase (ManSS11) from newly isolated Klebsiella pneumoniae SS11 and its food stain (mannan based) removal efficiency. The enzyme, ManSS11 was stable over a wide range of pH and temperature. The highest activity of ManSS11 was observed at pH 9.0 and temperature, 70 °C, with t1/2 of 135.91 min at the same temperature while, >70% of its initial activity was retained at pH 7.0-10.6. It was purified to 5.50-fold homogeneity with a final recovery of 9.6% and a specificity of 7573.57 U/mg protein. Purified ManSS11 was visible as a single protein band with a molecular weight of ~45 kDa. The kinetic parameters of Km, Vmax and kcat were 1.66 mg/mL, 833.33 μmolmL-1 min-1 and 1190.47 s-1 respectively. The compatibility of β-mannanase with different detergents together with wash performance test confirmed its potential usability in laundry sector. Wash performance analysis confirmed that the enzyme displayed great efficiency in the removal of stains caused by mannan containing foods.Entities:
Keywords: Klebsiella pneumoniae; Locust bean gum; Mannanases
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Year: 2019 PMID: 31100392 DOI: 10.1016/j.ijbiomac.2019.05.067
Source DB: PubMed Journal: Int J Biol Macromol ISSN: 0141-8130 Impact factor: 6.953