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Correlation Between Enzyme Activity and Stability of a Protease, an Alpha‐Amylase and a Lipase in a Simplified Liquid Laundry Detergent System, Determined by Differential Scanning Calorimetry
Author(s) -
Lund Henrik,
Kaasgaard Svend Gunnar,
Skagerlind Peter,
Jorgensen Lene,
Jorgensen Christian Isak,
Weert Marco
Publication year - 2012
Publication title -
journal of surfactants and detergents
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.349
H-Index - 48
eISSN - 1558-9293
pISSN - 1097-3958
DOI - 10.1007/s11743-011-1272-5
Subject(s) - differential scanning calorimetry , chemistry , lipase , enzyme , chromatography , laundry , amylase , protease , enzyme assay , thermodynamics , biochemistry , physics , history , archaeology
Enzymes used during washing in laundry detergents have become a universal tool to lower energy consumption and to generate a broad, consumer‐relevant, cleaning effect. However, the stability of these enzymes remains a major obstacle, particularly in liquid products, due to increased interaction between the enzymes and the other components of the detergent. The process of formulation involves extensive shelf‐life stability studies where residual enzyme activities are correlated with formulation variations. As a way to improve the formulation process, we evaluated the possible use of differential scanning calorimetry (DSC) as a tool to predict enzyme stability in liquid detergents. Thus, residual enzyme activity after incubation in a multitude of formulations was determined and compared to thermodynamic data obtained by DSC. The enzymes tested were a protease, an alpha‐amylase and a lipase. We found a strong linear correlation between DSC‐derived data, in particular T max (temperature at peak maximum of the transition from the folded to unfolded state) and enzyme activity studies with R 2 ‐values: 0.98 (protease), 0.99 (amylase) and 0.98 (lipase), respectively. Thus, a higher T max for the same enzyme in a particular formulation is directly proportional to longer storage stability. These results suggest a new way of greatly accelerating this type of formulation study, allowing estimation of enzyme compatibility with a specific formulation on a daily, rather than the weekly or monthly basis used at present.