Arginine ethylester prevents thermal inactivation and aggregation of lysozyme
نویسندگان
چکیده
منابع مشابه
Thermal Inactivation and Aggregation of Lysozyme in the Presence of Nano- TiO2 and Nano-SiO2 in Neutral pH
Protein aggregation is a problem in biotechnology. High temperature is one of the most important reasons to enhance enzyme inactivation and aggregation in industrial systems. This work focuses on the effect of TiO2 and SiO2 nanoparticles on refolding and reactivation of lysozyme. In the presence of TiO2 and SiO2 nanoparticles, after enzyme heat treatm...
متن کاملthermal inactivation and aggregation of lysozyme in the presence of nano- tio2 and nano-sio2 in neutral ph
protein aggregation is a problem in biotechnology. high temperature is one of the most important reasons to enhance enzyme inactivation and aggregation in industrial systems. this work focuses on the effect of tio2 and sio2 nanoparticles on refolding and reactivation of lysozyme. in the presence of tio2 and sio2 nanoparticles, after enzyme heat treatment at 98◦c for 30 min, not only aggregates ...
متن کاملthermal aggregation of hen egg white lysozyme: effect of polyamines
protein aggregation is a serious problem for both biotechnology and cell biology. diseases such as prion misfolding, alzheimer’s, and other amyloidosis are phenomena for which protein aggregation in our living cells is of considerable relevance. human lysozyme has been shown to form amyloid fibrils in individuals suffering from nonneuropathic systemic amyloidosis, all of which have point mutati...
متن کاملRadiation-produced aggregation and inactivation in egg white lysozyme.
Chromatographically homogeneous egg white lysozyme has been subjected under reduced pressure to 0.67-m.e.v. y-rays. At 37% destruction of enzymic activity, three inactive aggregates and one partially active fraction have been isolated by salt precipitation and chromatographic procedures. The aggregates, upon reduction with 2-mercaptoethanol and reaction with iodoacetic acid, give derivatives wi...
متن کاملThermal Inactivation and Aggregation of Lysozyme in the Presence of Nano- TiO2 and Nano-SiO2 in Neutral pH
Protein aggregation is a problem in biotechnology. High temperature is one of the most important reasons to enhance enzyme inactivation and aggregation in industrial systems. This work focuses on the effect of TiO2 and SiO2 nanoparticles on refolding and reactivation of lysozyme. In the presence of TiO2 and SiO2 nanoparticles, after enzyme heat treatment at 98C for 30 min, not only aggregates w...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2004
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.2004.04257.x