title: Thermozymes and their applications: a review of recent literature and patents.
abstract: Enzymes from thermophilic microorganisms, thermozymes, have unique characteristics such as temperature, chemical, and pH stability. They can be used in several industrial processes, in which they replace mesophilic enzymes or chemicals. Thermozymes are often used when the enzymatic process is compatible with existing (high-temperature) process conditions. The main advantages of performing processes at higher temperatures are reduced risk of microbial contamination, lower viscosity, improved transfer rates, and improved solubility of substrates. However, cofactors, substrates, or products might be unstable or other side reactions may occur. Recent developments show that thermophiles are a good source of novel catalysts that are of great industrial interest. Thermostable polymer-degrading enzymes such as amylases, pullulanases, xylanases, proteases, and cellulases are expected to play an important role in food, chemical, pharmaceutical, paper, pulp, and waste-treatment industries. Considerable research efforts have been made to better understand the stability of thermozymes. There are no major conformational differences with mesophilic enzymes, and a small number of extra salt bridges, hydrophobic interactions, or hydrogen bounds seem to confer the extra degree of stabilization. Currently, overexpression of thermozymes in standard Escherichia coli allows the production of much larger quantities of enzymes, which are easy to purify by heat treatment. With wider availability and lower cost, thermophilic enzymes will see more application in industry.
authors: Department of Food Technology and Nutritional Sciences, Wageningen University, The Netherlands. marieke.bruins@algemeen.pk.wau.nl
authors: M E
authors: ME
authors: Bruins
authors: A E
authors: AE
authors: Janssen
authors: R M
authors: RM
authors: Boom
mesh_terms: D001105:Archaea / Q000201:enzymology*; D001419:Bacteria / Q000201:enzymology*; D004795:Enzyme Stability / Q000502:physiology / Q000528:radiation effects; D004798:Enzymes / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006358:Hot Temperature; D010330:Patents as Topic; D015202:Protein Engineering / Q000639:trends*; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics
chemical_list: D004798:Enzymes