Coatings World - May 2010

mately leads to creation of microorganisms designed to express enzymes that can achieve specific chemical reactions. Metabolic engineering tools enable researchers to improve the microorganisms that are used to produce the enzymes and aim to affect metabolic pathways to achieve higher yields while reducing energy consumption and waste generation. When combined, these technologies make it possible to design commercially viable biocatalysts with specific properties targeted for application as additives in paints and coatings.

ARE YOU READY TO FUNCTIONALIZE AND IMPROVE YOUR PRESENT FORMULATIONS? As the paint and coatings industry recovers from the recession, analysts predict that significant consolidation will ensue. Companies lacking differentiating technologies and notable value-added formulations may not survive the fierce competition. Bioengineered additives can enable coatings suppliers to develop sustainable coating solutions with unique functionalities. You don’t have to break the bank to achieve differentiation, you can just functionalize your formulations.

What functionalities do you want to bring to your future product lines?

With its present range of available products and broad portfolio of other additives under development, Reactive Surfaces has successfully demonstrated the viability of biobased additives as a means of introducing novel activity to surfaces. We have the unique combination of expertise and capabilities in biotechnology and coatings formulation to identify further candidates and functionalities you need. Forward-thinking manufacturers will seriously investigate the advantages of integrating such bioadditives into their coating products, including functionalities highlighted in these articles as well as those not yet discussed. We are eager to work with such market leaders to explore all of the possible opportunities presented by nature, and in doing so to help you reinvigorate the coatings industry. CW

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Table 3: Lipolytic Enzymes
Enzyme
Enzyme
Commission
Catalyzed Reaction(s) and Availability of Thermophilic Enzymes

Carboxylesterase

3.1.1.1

carboxylic ester + H2O = an alcohol + a carboxylate (e.g., a fatty acid of 10 or less carbons);
thermophilic carboxylesterases have been obtained from Aeropyrum pernix, Alicyclobacillus
acidocaldarius, Archaeoglobus fulgidus, Bacillus acidocaldarius, Pseudomonas aeruginosa,
Sulfolobus shibatae, Sulfolobus solfataricus, and Thermotoga maritime
Lipase

3.1.1.3

triacylglycerol + H2O = diacylglycerol + a carboxylate (e.g., a fatty acid of 12 or more carbons);
themophilic lipases have been obtained from Acinetobacter calcoaceticus, Acinetobacter sp.,
Bacillus sphaericus, Bacillus stearothermophilus, Bacillus thermocatenulatus, Bacillus ther-
moleovorans, Candida rugosa, Candida thermophila, GeoBacillus thermoleovorans Toshki,
Pseudomonas fragi, Staphylococcus xylosus, and Sulfolobus solfataricus
Acylglycerol lipase

3.1.1.23

glycerol monoester + H2O = glycerol + a carboxylate
Phosphatidylinositol
deacylase

3.1.1.52

1-phosphatidyl-D-myo-inositol + H2O = 1-acylglycerophosphoinositol + a carboxylate Phospholipase C

3.1.4.3

phosphatidylcholine + H2O = 1,2-diacylglycerol + choline phosphate; a thermophilic
phospholipase C has been obtained from Bacillus cereus
Lysophospholipase