Background: D-Phenylglycine aminotransferase (D-PhgAT) is highly beneficial in pharmaceutical biotechnology. Like many other enzymes, D-PhgAT suffers from low stability under harsh processing conditions, poor solubility of substrate, products and occasional microbial contamination. Incorporation of miscible organic solvents into the enzyme’s reaction is considered as a solution...

Attempts to resolve the question of the identity or non-identity of the so-called staphylococcus toxins have made use of tests of thermostability, without, however, leading to any general agreement as to the heat-resistance of any of the particular toxic fractions. Nor have these tests revealed the essential nature of the substances concerned in the different manifestations of toxic action. The...

To probe noncovalent interactions within the collagen triple helix, backbone amides were replaced with a thioamide isostere. This subtle substitution is the first in the collagen backbone that does not compromise thermostability. A triple helix with a thioamide as a hydrogen bond donor was found to be more stable than triple helices assembled from isomeric thiopeptides.

Identifying determinant(s) of protein thermostability is key for rational and data-driven protein engineering. By analyzing more than 130 pairs of mesophilic/(hyper)thermophilic proteins, we identified the quality (residue-wise energy) of hydrophobic interactions as a key factor for protein thermostability. This distinguishes our study from previous ones that investigated predominantly structur...

Design of thermally stable proteins is spurred by their applications in bionanotechnology. There are three major issues governing this: first, the upper limit on the temperature at which proteins remain physiologically active and are available for technological applications (answers may emerge from the discovery of new, natural hyperthermophilic enzymes that are active above 125 degrees C or fr...

For most multidomain proteins the thermal unfolding transitions are accompanied by an irreversible step, often related to aggregation at elevated temperatures.As a consequence the analysis of thermostabilities in terms of equilibrium thermodynamics is not applicable, at least not if the irreversible process is fast with respect the structural unfolding transition. In a comparative studywe inves...

(HOROWITZ and SHEN 1952). The strain produces almost no tyrosinase activity when cultured at 35" C on a medium which favors the production of strong activity in 25" cultures. The evidence indicated that the temperature effect is not due to formation of a tyrosinase inhibitor, but to a net decrease in tyrosinase synthesis at the higher temperature. Attention has been called to the resemblance be...