STUDY of Enzyme Formulations Involving
Bovine β-trypsin with greater activity and stability
Depending on the Ion Concentration to Act In
Commercial detergent and soap systems
Name: ANTONIO VICTOR BAIOCO VASCONCELOS
Publication date: 24/06/2020
Advisor:
Name |
Role |
|---|---|
| ALEXANDRE MARTINS COSTA SANTOS | Advisor * |
Examining board:
| Name |
Role |
|---|---|
| ALEXANDRE MARTINS COSTA SANTOS | Advisor * |
| LUCAS CUNHA DIAS DE REZENDE | Internal Examiner * |
Summary: Household cleaning is a daily worldwide activity, which means that billions of people
use detergents to clean their clothes, dishes, and so forth. The enzymes are
increasingly added to achieve "catalytic cleaning", thereby creating smaller fragments
of the stain constituents, which in turn facilitates the chemical cleaning action of
surfactants. Household detergents are the most important application of industrial
enzymes, representing 50% of total sales. Much progress has been made in the last
decades in elucidating the structure function relations of enzymes. In this
experimental work, we developed a physicochemical study and the biological
properties of the bovine β-trypsin isoform related to the concentration of ions that can
be used in the formulation of detergents. The enzyme activity of the β-trypsin isoform
shown to be influenced by the concentration of cations, but no significant change was
observed for anions in the range from 0 to 20 mmol⋅L
-1
. For the ionic series of
cations, the metallic calcium ion was more effective, but at low concentration from 5
to 10 mmol⋅L
-1
, differently from what has been reported in the literature for the
interaction of this ion with the enzyme. The monitoring of the effect of the Ca2+ ion on
the protein conformation by fluorescence spectroscopy in an acid medium showed
that the conformational changes induced in the structure are considered
conformational adjustments or small structural adjustments, that not inducing an
increase in the fraction of denatured molecules. The thermodynamic analysis of the
enzyme system under the influence of the CaCl2 showed that the changes caused by
the addition of calcium chloride up to 20 mmol⋅L
-1
act mainly on the thermodynamic
parameters of cooperativity and heat capacity decreasing both. Furthermore, the
addition of calcium ions above the concentration of 5 mmol⋅L
-1 has a pronounced
effect on protein destabilization. Thus, the typical concentrations of 20 mmol⋅L
-1 were
destabilizing in both systems tested. Thus, with the determination of the biological
and physical-chemical parameters in relation to the enzyme with ions in solution, and
mainly the thermodynamics, we can start the second phase of the work that is the
formulation of the detergent system with β-trypsin isoform.
