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Introduction Recombinant proteins first came to light in 1970’s. The method was initially proposed by a graduate student called Peter Lobban. It was then acknowledged by two scientists called Stanley...

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Recombinant proteins first came to light in 1970’s. The method was initially proposed by a
graduate student called Peter Lobban. It was then acknowledged by two scientists called
Stanley Norman Cohen and Herbert Boyer, who went on to publicize their work. Herbert
Boyer then went on to use this recombinant technology to create the first recombinant drug,
a biosynthetic human insulin product (Berg and Mertz, 2010).
These proteins are coded for by a recombinant DNA sequence. This technology allows us to
cut different fragments of DNA from different sources so that they could later be combined to
create a recombinant DNA strand. These new DNA strands could be used in a multitude of
ways and changed how scientists could analyse and manipulate biological molecules. The
revelation of this technology led to many breakthroughs and discoveries, some of which I will
cover later

Answered Same Day Oct 14, 2019 BMS3092


David answered on Dec 28 2019
144 Votes
“Recombinant proteins are important in the 21st century?”
“Recombinant proteins” are manipulated form of proteins that are encoded by “recombinant DNA” molecules using biomolecular engineering. These “Recombinant DNAs” are generated by using “Recombinant technology”. In “Recombinant technology”, DNA molecules from at-least two different species are joined together to
ing genetic material from multiple sources creating such sequence that are not found in genome under natural conditions. The joining is done by inserting them into a host organism such as bacteria, yeast, or mammalian cells to create new genetic combinations which are for medical, academic and research uses.
The method of “Recombinant DNA” was developed during seventies of 20th Century (1970 to 1979). In the starting of the decade, a graduate student, Peter Lo
an, initially planned this method along with a biochemist, A. Dale Kaiser at Stanford University. The method was later acknowledged by two scientists called Stanley Norman Cohen and He
ert Boyer when their predictions were published in a journal named "Enzymatic end-to-end joining of DNA molecules" in 1973. The method reached at a new advanced level in 1977 with creation of the biosynthetic "human" insulin by He
ert Boyer, which was the first recombinant drug.
For the purpose of this assignment, I would write this essay in such a way that it would cover advantages, challenges of using recombinant proteins along with its contribution in the area of medicine, scientific research and the food industry. At the end, we would conclude whether or not recombinant proteins are important in 21st century.
Creation of Recombinant Protein
Recombinant DNAs are produced by one of the two ways; “Molecular Cloning” & “Polymerase Chain Reaction”. Under the molecular cloning, one molecule is replicated to a population of cells with identical DNA molecules by using DNA sequences from different organisms of the source species (i.e. source of the DNA to be cloned) and the living host for replication of the recombinant DNA. Wherein, under PCR technique, a single copy or a few copies of a segment of DNA is amplified across several orders of magnitude that generate thousands to millions of copies of that specific DNA sequence.
When we look for the differences between these two methods, we would find two fundamental differences;
(i) In “Molecular cloning”, DNAs are replicated within a living cell whereas in “PCR” DNAs are replicated in a test tube that is free of living cells.
(ii) DNA sequences are copied and pasted in “Molecular cloning” whereas they are amplified by copying their existing sequence under “PCR”.
Advantages of Recombinant Protein
The emergence of “Recombinant Proteins” has
ought number of advancements in the fields of food & agriculture and medicines. The major benefits using these proteins are;
(a) Purity percentage of these proteins is quite high compared to other methods when the required proteins are not easily available from a natural system. This makes Recombinant proteins a better product compared to the previous ones.
(b) The supply of these proteins is continuous with high yields which wasn’t the case previously. This helps in fulfilling the demand of the market i
espective of demand levels.
(c) Producing peptides using Recombinant protein is cheaper than chemical synthesis.
(d) Recombinant proteins can provide type of proteins that do not exist naturally.
(e) Production of Recombinant proteins shows high level of consistency in batch to batch production.
(f) These proteins are easier to be modified which helps in improvement of mutant versions of known proteins.
(g) Recombinant proteins much more freedom in creation of a new protein as any DNA sequence can be used in production of these proteins. This results in higher specificity of the proteins.
Challenges faced in the production of Recombinant Protein:
Recombinant proteins have experienced a surge in demand in recent decades due to the higher number of applications of recombinant proteins in different fields gaining commercial grounds. As per, as of today there are more than 75 recombinant proteins being used as pharmaceuticals and there are more than 360 new medicines that are being developed based on these proteins. However, production of these proteins still constitutes a challenge that need to be taken care.
One of the major challenges related to production of recombinant protein is “loss of expression”. Efficient expression of the gene of interest is a necessary condition in order to produce adequate recombinant protein. However, there always exists a possibility of “loss of these expressions” that can be lost because of structural changes in the recombinant gene or dissolution of the gene from host cells. The major issues related to “loss of expression” are Codon bias & Aggregation of protein. Another challenge associated with production of Recombinant protein is “Protein toxicity”. When these proteins perform a function that creates an interference with the homeostasis of the host cell, there is a possibility of “Protein toxicity” that would most probably slower down the growth rate and at extreme, cell death.
Proper formation of disulphide bonds is an important aspect of the production of most recombinant proteins. If this formation is disrupted or not done in a proper manner, it could result into misfolding and the formation of inclusion bodies.
Pharmaceutical Products based on Recombinant Protein:
There are certain proteins that could be utilized as pharmaceutical agents for the treatment of many human...

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