GiveMe Shelter: a people-centred design process for promoting independent inquiry-led learning in engineering

It has become increasingly common for tasks traditionally carried out by engineers to be undertaken by technicians and technologist with access to sophisticated computers and software that can often perform complex calculations that were previously the responsibility of engineers. Not surprisingly, this development raises serious questions about the future role of engineers and the education needed to address these changes in technology as well as emerging priorities from societal to environmental challenges. In response to these challenges, a new design module was created for undergraduate engineering students to design and build temporary shelters for a wide variety of end users from refugees, to the homeless and children. Even though the module provided guidance on principles of design thinking and methods for observing users needs through field studies, the students found it difficult to respond to needs of specific end users but instead focused more on purely technical issues.

Rational design of a (S)-selective-Transaminase for asymmetric synthesis of (1S)-1-(1,1'-biphenyl 2-yl)ethanamine

Amine transaminases offer an environmentally sustainable synthesis route for the production ofpure chiral amines. However, their catalytic efficiency towards bulky ketone substrates isgreatly limited by steric hindrance and therefore presents a great challenge for industrialsynthetic applications. Hereby we report an example of rational transaminase enzyme design tohelp alleviate these challenges. Starting from the Vibrio fluvialis amine transaminase that has nodetectable catalytic activity towards the bulky aromatic ketone 2-acetylbiphenyl, we employed arational design strategy combining in silico and in vitro studies to engineer the transaminaseenzyme with a minimal number of mutations, achieving an high catalytic activity and highenantioselectivity. We found that by introducing two mutations W57G/R415A detectableenzyme activity was achieved. The rationally designed best variant,W57F/R88H/V153S/K163F/I259M/R415A/V422A, showed an improvement in reaction rateby > 1716-fold towards the bulky ketone under study, producing the corresponding enantiomericpure (S)-amine (ee value of > 99%).