نتایج جستجو برای: catalytic enzymes

تعداد نتایج: 197119  

2015
Joyeeta Mukherjee Munishwar Nath Gupta

Enzymes require some flexibility for catalysis. Biotechnologists prefer stable enzymes but often this stabilization comes at the cost of reduced efficiency. Enzymes from thermophiles have low flexibility but poor catalytic rates. Enzymes from psychrophiles are less stable but show good catalytic rates at low temperature. In organic solvents enzymes perform poorly as the prior drying makes the e...

Journal: :Materials advances 2022

A strategy of using nano-carbons to mimic the catalytic behaviour enzymes is put forward.

Background: Considering natural thermal stability, Geobacillus stearothermophilus amylase and Cel5E from Clostridium thermocellum are good candidates for industrial applications. To be compatible with the industrial applications, this enzyme should be stable in the high temperatures, so any improvement in their thermal stability is valuable.Objectives: Us...

Journal: :Journal of the American Chemical Society 1908

Journal: :Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie 1977
W Gruber B Zapf K H Schrappe R Linke

Enzyme preparations used for quality control of enzyme activity determinations in clinical chemistry should be very similar to human enzymes. Antibodies against e.g. porcine enzymes show cross reactivity with the corresponding human enzymes, indicating partial identity of the enzyme proteins. As the enzyme-antibody precipitates retain catalytic activity the similarity between the enzyme protein...

2015
Priyadarshini P. Pai S. S. Shree Ranjani Sukanta Mondal Narayanaswamy Srinivasan

Identification of catalytic residues can help unveil interesting attributes of enzyme function for various therapeutic and industrial applications. Based on their biochemical roles, the number of catalytic residues and sequence lengths of enzymes vary. This article describes a prediction approach (PINGU) for such a scenario. It uses models trained using physicochemical properties and evolutiona...

2011
Kayoko M. Fukasawa Toshiyuki Hata Yukio Ono Junzo Hirose

Almost all naturally occurring metalloproteases are monozinc enzymes. The zinc in any number of zinc metalloproteases has been substituted by some other divalent cation. Almost all Co(II)- or Mn(II)-substituted enzymes maintain the catalytic activity of their zinc counterparts. However, in the case of Cu(II) substitution of zinc proteases, a great number of enzymes are not active, for example, ...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید