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Virgibacillus dokdonensis VITP14 produces α-amylase and protease with a broader operational range but with differential thermodynamic stability
S. Mishra, N.N. Joghee,
Published in Blackwell Publishing Ltd
PMID: 33289126
Extracellular α-amylase and protease were coproduced from halo tolerant Virgibacillus dokdonensis VITP14 with banana peels (2% w/v) as substrate. The pH optima for α-amylase and protease were 6.5 and 7.0, respectively. The temperature optima of α-amylase and protease were 30 and 50 °C, respectively. Both the enzymes were active in the presence of various metal ions (1 mM of Ni2+, Ca2+, Ba2+, Sr2+, and Mg2+), detergents (Tween 20, Tween 80, Triton X-100), and other additives (2-mercaptoethanol and urea). Both the enzymes followed Michaelis–Menten type enzyme kinetics with Vmax of 121.40 and 4.17 μmol Min−1 mL−1 and Km of 0.59 and 0.28 mg mL−1 for amylase and protease, respectively. Amylase showed higher activation energy for inactivation (75.55 kJ mol−1 compared to 59.70 kJ mol−1 for protease) and higher thermal stability (reflected by longer half-life 53.23 Min compared to 0.11 Min for protease) at 60 °C. The coexistence of amylase and protease could be attributed to the difference in the optimum temperatures of activity and thermal stability of the two enzymes. © 2020 International Union of Biochemistry and Molecular Biology, Inc.
About the journal
JournalBiotechnology and Applied Biochemistry
PublisherBlackwell Publishing Ltd