Improving the thermostability of horseradish peroxidase by incorporating into water-immiscible coacervates

dc.contributor.authorКороткова, Ірина Валентинівна
dc.date.accessioned2019-03-17T16:16:09Z
dc.date.available2019-03-17T16:16:09Z
dc.date.issued2018
dc.description.abstractLooking for novel matrix materials for encapsulation of enzymes based on waterimmiscible coacervates prepared by reaction of negatively charged hyaluronic acid and a positively charged recombinant mussel adhesive protein containing tyrosine residues was the subject of the investigation of this work. The results of experimental study of the thermostability of horseradish peroxidase (HRP) by means its encapsulation in these coacervates at temperature from 30 to 95 C is presented in this paper. The Michaelis- o Menten equation was applied to analyze of the enzymatic activity of HRP. The kinetic parameters were interpreted using a Lineweaver-Burk plot. According to the data obtained, Michaelis-Menten parameters, K and K , interpreted from the Lineweaver- M Cat Burk plots, were 0.271 mM and 2265 s for the free HRP and 0.325 mM and 2158 s for the -1 -1 rMAP/HA coacervate, containing HRP, respectively, which indicate that the enzyme did not lose its activity during the coacervate formation. It was founded that the free enzyme began to lose activity above 40 C, while the encapsulated HRP remained stable to 85 C. o o The encapsulated HRP lost only 18% and 25% of activity at temperature of 90 and 95 C, o respectively, while as free HRP loses all its initial activity, although they show similar activity at room temperature.uk_UA
dc.identifier.doiDOI: https://dx.doi.org/10.4314/njb.v35i2.4
dc.identifier.urihttps://dspace.pdau.edu.ua/handle/123456789/4404
dc.language.isoen_USuk_UA
dc.publisherNIGERIAN JOURNAL OF BIOTECHNOLOGYuk_UA
dc.relation.ispartofseries;Vol. 35 No. 2 (2018): 27-34
dc.subjectencapsulation, hyaluronic acid, coacervate, recombinant mussel adhesive proteinuk_UA
dc.titleImproving the thermostability of horseradish peroxidase by incorporating into water-immiscible coacervatesuk_UA
dc.title.alternativeImproving the thermostability of horseradish peroxidase by incorporating into water-immiscible coacervatesuk_UA
dc.typeArticleuk_UA
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