Cold-active enzymes constitute an attractive resource for biotechnological applications. Their high catalytic activity at temperatures below 25° C makes them excellent biocatalysts …
C Ortiz, ML Ferreira, O Barbosa… - Catalysis Science & …, 2019 - pubs.rsc.org
Novozym 435 (N435) is a commercially available immobilized lipase produced by Novozymes. It is based on immobilization via interfacial activation of lipase B from Candida …
RK Singh, MK Tiwari, R Singh, JK Lee - International journal of molecular …, 2013 - mdpi.com
Enzymes found in nature have been exploited in industry due to their inherent catalytic properties in complex chemical processes under mild experimental and environmental …
By far the largest proportion of the Earth's biosphere is comprised of organisms that thrive in cold environments (psychrophiles). Their ability to proliferate in the cold is predicated on a …
The bulk of the Earth's biosphere is cold (eg 90% of the ocean's waters are≤ 5° C), sustaining a broad diversity of microbial life. The permanently cold environments vary from …
Lipases are glycerol ester hydrolases that catalyze the hydrolysis of triglycerides to free fatty acids and glycerol. Lipases catalyze esterification, interesterification, acidolysis, alcoholysis …
Chirality is a key factor in the safety and efficacy of many drug products and thus the production of single enantiomers of drug intermediates and drugs has become important …
Y Xie, J An, G Yang, G Wu, Y Zhang, L Cui… - Journal of Biological …, 2014 - ASBMB
Enzyme stability is an important issue for protein engineers. Understanding how rigidity in the active site affects protein kinetic stability will provide new insight into enzyme …
R Kazlauskas - Chemical Society Reviews, 2018 - pubs.rsc.org
Protein function requires the folded protein form, but this form is unstable mainly because it readily unfolds into a flexible, unstructured form. Protein folding is favored by burying of …