Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins.

Apo and holo forms of lactoferrin (LF) from caprine and bovine species have been characterized and compared with regard to the structural stability determined by thermal denaturation temperature values (T (m)), at pH 2.0-8.0.

Effect of cosolvents on the structural stability of endoglucanase from Aspergillus aculeatus.

The effects of cosolvents such as sucrose, glycerol, and sorbitol on endoglucanase have been studied by activity, circular dichroic spectroscopy, fluorescence, and apparent thermal transition temperature measurements. The endoglucanase activity increased by 4-fold at 40% cosolvent concentration under optimum conditions. The endoglucanase lost 50% of its activity when exposed to 90 degrees C for more than 30 min (1 h).

Influence of polyols on the stability and kinetic parameters of invertase from Candida utilis: correlation with the conformational stability and activity.

Invertase (beta-D -fructofuranoside fructohydrolase-E.C. 3.

Purification, characterization, and solvent-induced thermal stabilization of ficin from Ficus carica.

Ficin (EC 3.4.22.

Effect of cosolvents on the stabilization of bioactive peptides from bovine milk alpha-casein.

Peptides with more than one biological activity are many a times multifunctional peptides. Two peptides with multifunctional properties from alpha (S2)-casein were stabilized in presence of cosolvents for their biological activities like ACE inhibition activity and antioxidant activity. These bioactive peptides in cosolvents were also thermostable.

Purification and characterization of a new endoglucanase from Aspergillus aculeatus.

Endoglucanase has been isolated from Aspergillus aculeatus. The purified enzyme showed a single band and had a molecular weight of 45,000 Da as indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, with a specific activity of 1.4 units/mg.