Erickson, B., Nelson, J.E. & Winters, P. Perspective on opportunities in industrial biotechnology in renewable chemicals. Biotechnol. J. 7(2), 176–185

Biotechnology Industry Organization (BIO), Washington, DC, USA.
Biotechnology Journal (Impact Factor: 3.49). 02/2012; 7(2):176-85. DOI: 10.1002/biot.201100069
Source: PubMed


From biomass to renewable chemicals: while industrial biotechnology offers a clear value proposition, a number of hurdles need to be addressed to fully realize the commercial potential of bio-based products and chemicals over the coming decade. A review of an early roadmap for biological production of chemicals from renewable sugars reveals a focus on those that would provide co-products for integrated biorefineries producing biofuels and bioenergy. A growing number of companies are now focusing on specialty chemicals as an entry point to build the bio-based economy.

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    • "Enzymes have over the course of the last decade established themselves as useful alternatives to classical organo-and metallo-catalysis (Anastas and Warner, 1998; Bornscheuer et al., 2012; Illanes et al., 2012; Meyer, 2011). They are increasingly employed for the manufacturing of a diverse array of chemical products such as pharmaceuticals, agrochemicals, bulk chemicals or biofuels on preparative as well as industrial scale (Erickson et al., 2012). This focus also applies to biological degradation of products, such as xenobiotics, plastics, biomass and unwanted components in wastewater (Cammarota and Freire, 2006; Eberl et al., 2008; Janssen et al., 2005; Kullman and Matsumura, 1996; Müller et al., 2005; Rabinovich et al., 2004; Ribitsch et al., 2012). "
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    ABSTRACT: Enzyme catalyzed processes are increasingly complementing chemical manufacturing as new enzymes are being discovered. Although many industrially applied biocatalysts have been identified by functional screenings technological advances in the -omics fields have created a different path to access novelty. Here we describe how -omics technologies, especially proteomics and transcriptomics, can complement each other in the aim of finding new enzymatic functions. Special emphasis is laid on how mRNA sequencing Zcan improve proteomic experiments by allowing the generation of high quality protein sequence databases, which subsequently facilitates protein identification.
    Full-text · Article · Dec 2015 · Journal of Biotechnology
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    • "The development of green chemical techh nologies causes a significant decrease of the negative anthropogenic effect on environment, appearance of environmenttfriendly technological processes, and sustainable use of natural resources. Today, in some countries, biotechnological production of bioethanol, polylactic acid, and 1,33propanediol is being carried out successfully (Erickson et al., 2012). Development of cheap substrates that do not compete with food stuffs for the cultivation of microorganisms is one of the possible ways of reducing the costs of biotechnoo logical production. "

    Full-text · Dataset · Oct 2015
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    • "The genomic and metabolic diversity of prokaryotic domains of life is an extraordinary source for the development of innovative bio-based products of a high application value (Erickson et al. 2012; Buschke et al. 2013; Cragg and Newman 2013; He et al. 2014; Yu 2014). Marine environments contain an exceptional biodiversity generated and supported by a diversified range of special substrates and extreme conditions, such as high and low temperatures, extreme pH values, elevated salinities, pressure, and even irradiation. "
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    ABSTRACT: A metagenomic fosmid expression library established from environmental DNA (eDNA) from the shallow hot vent sediment sample collected from the Levante Bay, Vulcano Island (Aeolian archipelago) was established in Escherichia coli. Using activity-based screening assays, we have assessed 9600 fosmid clones corresponding to approximately 350 Mbp of the cloned eDNA, for the lipases/esterases/lactamases, haloalkane and haloacid dehalogenases, and glycoside hydrolases. Thirty-four positive fosmid clones were selected from the total of 120 positive hits and sequenced to yield ca. 1360 kbp of high-quality assemblies. Fosmid inserts were attributed to the members of ten bacterial phyla, including Proteobacteria, Bacteroidetes, Acidobateria, Firmicutes, Verrucomicrobia, Chloroflexi, Spirochaetes, Thermotogae, Armatimonadetes, and Planctomycetes. Of ca. 200 proteins with high biotechnological potential identified therein, we have characterized in detail three distinct alpha/beta-hydrolases (LIPESV12_9, LIPESV12_24, LIPESV12_26) and one new alpha-arabinopyranosidase (GLV12_5). All LIPESV12 enzymes revealed distinct substrate specificities tested against 43 structurally diverse esters and 4 p-nitrophenol carboxyl esters. Of 16 different glycosides tested, the GLV12_5 hydrolysed only p-nitrophenol-alpha-(l)-arabinopyranose with a high specific activity of about 2.7 kU/mg protein. Most of the alpha/beta-hydrolases were thermophilic and revealed a high tolerance to, and high activities in the presence of, numerous heavy metal ions. Among them, the LIPESV12_24 was the best temperature-adapted, retaining its activity after 40 min of incubation at 90 A degrees C. Furthermore, enzymes were active in organic solvents (e.g., > 30 % methanol). Both LIPESV12_24 and LIPESV12_26 had the GXSXG pentapeptides and the catalytic triads Ser-Asp-His typical to the representatives of carboxylesterases of EC
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