Editorial Upstream and Downstream of Recombinants

EditorialUpstream and Downstream of RecombinantsBiomolecules to Health Care Industry

Priscila G. Mazzola,1 Arthur Cavaco-Paulo,2 Jorge G. Farías,3 and Jorge F. B. Pereira4

1Faculty of Pharmaceutical Sciences, University of Campinas (UNICAMP), 13083-859 Campinas, SP, Brazil2Departamento de Engenharia Biologica, Universidade do Minho, Campus de Gualtar, 4710-057 Braga, Portugal3Facultad de Ingenierıa y Ciencias, Departamento de Ingenierıa Quımica, Universidad de la Frontera, Casilla 54-D, Temuco, Chile4School of Pharmaceutical Sciences, Universidade Estadual Paulista (UNESP), 14800-903 Araraquara, SP, Brazil

Correspondence should be addressed to Priscila G. Mazzola; [email protected]

Received 7 June 2016; Accepted 7 June 2016

Copyright © 2016 Priscila G. Mazzola et al. This is an open access article distributed under the Creative Commons AttributionLicense, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properlycited.

Biotechnology processes are the unique feasible way for theproduction of some pharmaceutical active principles. Thus,developments in molecular biology, recombinant techniques,separation, and purification methods have a primordialrole because of the innovative characteristic and economicimpact in obtaining these new drugs through biotechno-logical approaches. This special issue compiles a series ofrelevant studies on different biotechnological fields and appli-cations, reporting up-to-date developments on downstreamand upstream biopharmaceuticals.

Summarizing the results reported in the manuscriptspublished here, our readersmay find further insights througha series of fields, from the most fundamental geneticapproaches to the general aspects of biological and biochem-ical engineering. A complete study proposed by S. Zhang etal. applied next-generation RNA sequencing and developed amethod to analyse themutation rate of themRNA of Chinesehamster ovary producing monoclonal antibodies, which arewidely used for the production of biological therapeutics.Following the concept of monoclonal antibodies, E. Sasso etal. have presented a research study where they expanded theavailability of monoclonal antibodies interfering with hepati-tis C infection in hepatocytes. The results of these authorsreport an effective sequencing approach for library screening,demonstrating the successful conversion of recovered clonesto active immunoglobulins.This novel approach allows rapidand cheap isolation of antibodies for virtually any native

antigen involved in human diseases, for therapeutic and/ordiagnostic applications.

On the other hand, to clone and express 𝛾-polyglutamicacid (𝛾-PGA) synthetase gene in B. subtilis, B. Lin et al.have constructed a plasmid, which allowed the recombinantmicroorganism the synthesis of 𝛾-PGA into the fermentationbroth. This approach has potential industrial applicationssince 𝛾-PGA is a new water-soluble biodegradable anionicpolypeptide and, due to its interesting properties, such asnontoxicity, edibility, adhesiveness, film forming, and mois-ture retention capability, it can be a key compound for thehealth care industries. Also R. Niu and X. Chen reported afull-length cDNA, prokaryotic expression, and antimicrobialactivity of cloned haemoglobin (Hb) fromUrechis unicinctus,a marine spoon worm and economically important seafood.Their results elucidate the structure and potential functionof Hb, which may help to understand the immune defensemechanism of invertebrates and to give some new insightsinto antimicrobial peptides for drug discovery and diseasecontrol in U. unicinctus aquaculture. Following the sameconcept, in “Enhanced and Secretory Expression of HumanGranulocyte Colony Stimulating Factor by Bacillus subtilisSCK6,” S. Bashir et al. describe a simplified approach forenhanced expression and secretion of granulocyte colonystimulating factor (GCSF), a human cytokine, in the culturesupernatant of B. subtilis SCK6 cells. Their results haveshown that after expression and purification the protein has

Hindawi Publishing CorporationBioMed Research InternationalVolume 2016, Article ID 9374847, 2 pageshttp://dx.doi.org/10.1155/2016/9374847

2 BioMed Research International

a biological activity similar to the commercial preparationof GCSF. The last two works of this issue are aimed at theevaluation of stability of biomolecules and their accuratequantification, respectively. Formulating appropriate storageconditions for biopharmaceutical proteins is essential forensuring their stability and thereby their purity, potency,and safety over their shelf life. With that in mind B. K.Chavez et al. employed a model murine IgG3 produced in abioreactor and evaluated multiple formulation compositions.These studies have evaluated the antibody stability in a seriesof conditions using an experimental design approach, anoptimized formulation being identified in which the stabilitywas substantially improved under long-term storage condi-tions and after multiple freeze/thaw cycles. The last work isfocused on the importance of proteases in the biotechno-logical and pharmaceutical industries, and, consequently, thedetermination of optimum conditions and the developmentof a standard protocol are critical during selection of a reliablemethod to determine its bioactivity. With that in mind, D. F.Coelho et al. employed a quality control theory to validate amodified version of a method proposed in 1947, presentinga validated protocol that offers a significant improvement,given that subjective definitions are commonly used in theliterature and this simple mathematical approach makes itclear and concise.

The quality of the results and protocols compiled in thisissue have caught our interest, and we hope that these willhelp researchers and biotechnology-related professionals todevelop more exciting science regarding the improvementof the human health and the sustainability and safety of thebiotechnological industry.

Priscila G. MazzolaArthur Cavaco-Paulo

Jorge G. FarıasJorge F. B. Pereira

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Editorial Upstream and Downstream of Recombinants