Abstract
Conjugating bovine trypsin with oligosaccharides maltotriose, raffinose and stachyose increased its thermostability and suppressed autolysis, without affecting its cleavage specificity. These conjugates accelerated the digestion of protein substrates both in solution and in gel, compared to commonly used unmodified and methylated trypsins.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Cattle
-
Cytochromes c / chemistry
-
Enzyme Stability
-
Fructose-Bisphosphate Aldolase / chemistry
-
Gels
-
Heating
-
Myoglobin / chemistry
-
Oligosaccharides / chemistry
-
Proteomics
-
Raffinose / chemistry
-
Serum Albumin, Bovine / chemistry
-
Solutions
-
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
-
Trisaccharides / chemistry
-
Trypsin / chemistry*
Substances
-
Gels
-
Myoglobin
-
Oligosaccharides
-
Solutions
-
Trisaccharides
-
stachyose
-
Serum Albumin, Bovine
-
maltotriose
-
Cytochromes c
-
Trypsin
-
Fructose-Bisphosphate Aldolase
-
Raffinose