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Protein & Peptide Letters
ISSN (Print): 0929-8665
ISSN (Online): 1875-5305
DOI: 10.2174/092986609789071270      Price:  $58

Cold-Adapted Esterases and Lipases: From Fundamentals to Application

Author(s): Donatella de Pascale, Guido di Prisco, Gennaro Marino and M. Luisa Tutino
Pages 1172-1180 (9)
Micro-organisms that thrive at low temperatures produce cold-adapted enzymes which display high catalytic efficiency, generally associated with low thermal stability. In the recent past, researchers and industries have focused the attention on cold-adapted enzymes, whose peculiar properties make them particularly interesting either for investigating stability/flexibility relationships, or for their potential application in industrial processes. Among these enzymes, lipases and esterases, have potential utilisations in a broad range of biotechnological applications. In fact, these biocatalysts represent the most widely used enzymes in biotechnology and organic chemistry. Modern methods of genetic engineering combined with growing knowledge of structure and function allow further adaptation to industrial needs and exploration of novel applications. Hence, in this review we attempt to offer an overview on some psychrophilic esterases and lipases; major details will be presented for ORF PSHAa0051 from Pseudoalteromonas haloplanktis TAC125, recently investigated by our team. In addition, potential biotechnological applications will be discussed.
α/βhydrolase, psychrophilic bacterial strain, Pseudoalteromonas haloplanktis TAC125
Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy