Molecular Dynamics of Thermoenzymes at High Temperature and Pressure: A Review

• Published in: The Protein Journal 2014-08, Vol.33 (4), p.369-376
• Main Authors: Abedi Karjiban, Roghayeh, Lim, Wui Zhuan, Basri, Mahiran, Abdul Rahman, Mohd Basyaruddin
• Format: Article
• Language: English
• Subjects: Analysis; Animal Anatomy; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Biochemistry; Bioorganic Chemistry; Chemistry; Chemistry and Materials Science; Detergents; Enzyme Stability; Enzymes; Food science; Geobacillus stearothermophilus; High pressure; High temperature; Histology; Hot Temperature; Lipase; Lipase - chemistry; Lipase - metabolism; Molecular biology; Molecular dynamics; Molecular Dynamics Simulation; Morphology; Organic Chemistry; Pressure; Protein Folding; Proteins
• ISSN: 1572-3887; 1573-4943; 1875-8355
• DOI: 10.1007/s10930-014-9568-8

Lipases are known for their versatility in addition to their ability to digest fat. They can be used for the formulation of detergents, as food ingredients and as biocatalysts in many industrial processes. Because conventional enzymes are frangible at high temperatures, the replacement of conventional chemical routes with biochemical processes that utilize thermostable lipases is vital in the industrial setting. Recent theoretical studies on enzymes have provided numerous fundamental insights into the structures, folding mechanisms and stabilities of these proteins. The studies corroborate the experimental results and provide additional information regarding the structures that were determined experimentally. In this paper, we review the computational studies that have described how temperature affects the structure and dynamics of thermoenzymes, including the thermoalkalophilic L1 lipase derived from Bacillus stearothermophilus . We will also discuss the potential of using pressure for the analysis of the stability of thermoenzymes because high pressure is also important for the processing and preservation of foods.