Why do people deny evolution?

whatever gloomy. We have a lotta fun with our fantasy. What dp you do for fun besides spanking the monkey??.

Expanding Nature's Catalytic Repertoire for a Sustainable Chemical Industry
Nature, the best chemist of all time, solves the difficult problem of being alive and enduring for billions of years, under an astonishing range of conditions. Most of the marvelous chemistry that makes life possible is the work of nature's macromolecular protein catalysts, the enzymes. By using enzymes, nature can extract materials and energy from the environment and convert them into self‐replicating, self‐repairing, mobile, adaptable, and sometimes even thinking biochemical systems. These systems are good models for a sustainable chemical industry that uses renewable resources and recycles a good fraction of its products. And biology is not just a model from which to draw inspiration: living organisms or their components can be efficient production platforms. In fact, I predict that DNA‐programmable microorganisms will be producing many of our chemicals in the not‐so‐distant future.

That most chemicals are made using synthetic processes starting from petroleum‐based feedstocks reflects the remarkable creativity of synthetic chemists in developing reaction schemes and catalysts that nature never discovered. Synthetic chemistry has given us an explosion of products, which feed, clothe, house, entertain, and cure us. Synthetic chemistry, however, struggles to match the efficiency and selectivity that biology achieves with enzymes. In many cases, synthetic processes rely on precious metals, toxic reagents and solvents, and extreme conditions, and they generate substantial amounts of unwanted byproducts. DNA‐programmable chemical synthesis using enzymes promises to improve on synthetic chemistry, particularly if we are able to expand biology's catalytic repertoire to include some of the most synthetically useful reactions, under physiological conditions and with earth‐abundant resources. Such clean, green chemistry might sound like pie in the sky, but enzymes already show how a protein can orient substrates for reaction, exclude water from an active site, activate a metal or simple organic cofactor, or suppress competing reactions to draw out new and admirable synthetic capabilities. Synthetic chemists have been drawing inspiration from biology for decades, and now is the time for protein engineers to use inspiration from synthetic chemistry to generate new enzymes that will improve on and replace synthetic catalysts and reaction pathways.1

Unfortunately, our understanding of the link between sequence and function lags well behind our desire for new enzymes. Given that our ability to predict protein sequences, or even just changes to a sequence, which reliably give rise to whole new, finely tuned catalytic activities is rudimentary at best, creating new enzymes capable of improving on current synthetic processes is a pretty tall order. We also dream of going beyond known chemistry to create enzymes that catalyze reactions or make products that are simply not possible with any known method, synthetic or otherwise. Requiring that these new enzymes assemble and function in cells, where they can be made at low cost and incorporated into synthetic metabolic pathways to generate a broader array of products, represents an even greater set of engineering constraints and challenges.

Nature's enzymes are the products of evolution, not design. By using generations of mutation and selection for fitness advantages, evolution allows organisms to continuously update and optimize their enzyme repertoires. New enzymes even appear in real time in response to challenges (e.g. the need to resist antibiotics or pesticides) or opportunities (e.g. the chance to occupy a new food niche by degrading recently introduced, manmade substances). I argue that the process that gave rise to all the remarkable biological catalysts in nature should be able to produce yet more. In the laboratory. Quickly. Advances in molecular biology over the past few decades—the ability to write, cut, and paste DNA and to have that DNA read and translated into proteins in recombinant organisms—have given us the ability to breed enzymes much like we breed sheep or sake yeast. We can direct the evolution of enzymes in the laboratory by requiring them to perform in ways that may not be useful to a bacterium but are useful to us. Directed evolution achieves these desirable functional outcomes while circumventing our deep ignorance of how sequence encodes them.

Directed evolution mimics evolution by artificial selection, and is accelerated in the laboratory setting by focusing on individual genes expressed in fast‐growing microorganisms. We start with existing proteins (sourced from nature or engineered), introduce mutations, and then screen for the progeny proteins with enhanced activity (or another desirable trait). We use the improved enzymes as parents for the next round of mutation and screening, recombining beneficial mutations as needed, and continuing until we reach the target level of performance.

Engineering enzymes in the 1980s and 1990s, I learned the hard way that there was no reliable method to predict performance‐enhancing mutations. Turning instead to random mutagenesis and screening, I quickly realized that such mutations were easy to find and accumulate with the right evolutionary optimization strategy. My students and I observed that proteins, the products of evolution, are themselves readily evolvable. Properties we and others targeted in the early days of directed evolution (the mid‐1990s) included recovering activity in unusual environments (e.g. organic solvents), improving activity on non‐native substrates, enhancing thermostability, and changing enantioselectivity. We learned the then‐surprising fact that beneficial mutations could be far from an active site, and often appeared on the protein surface (which in those days was generally deemed insensitive to mutation and functionally neutral). To this day, no one can explain satisfactorily how such mutations exert their effects, much less predict them.

You seem to have a problem with what I wrote?

Hell NO. I often pull it up and post some of your **** at the interdisciplinary lab .They have a "Creationist Board" that has a contest for the goofiest posts on the interweb. They award a prrize every April Fools. Hold on, e have several months to go but youre in the running.
Its your maniacal style that is garnering the votes.

but you wrap yourself in Creationist arguments. "Quack Quack"

From your snippet:
Directed evolution achieves these desirable functional outcomes while circumventing our deep ignorance of how sequence encodes them.