Stabilization of free and immobilized enzymes using hyperthermophilic chaperonin

• Published in: Journal of bioscience and bioengineering Vol. 101; no. 2; pp. 131 - 136
• Main Authors: Kohda, Jiro, Kawanishi, Hirofumi, Suehara, Ken-Ichiro, Nakano, Yasuhisa, Yano, Takuo
• Format: Journal Article
• Language: English
• Published: Amsterdarm Elsevier B.V 01.02.2006; Elsevier Science; Elsevier Limited
• Subjects: ALCOHOL DEHYDROGENASE; Alcohol Dehydrogenase - chemistry; Alcohol Dehydrogenase - metabolism; ALCOHOL DESHIDROGENASA; ALCOOL DESHYDROGENASE; archaea; Biological and medical sciences; Biotechnology; chaperonin; Chaperonins - chemistry; Chaperonins - metabolism; ENZIMAS INMOVILIZADAS; ENZYME IMMOBILISEE; Enzyme Stability; Enzymes, Immobilized - chemistry; Enzymes, Immobilized - metabolism; Fundamental and applied biological sciences. Psychology; Gels; heat stabilization; HEAT TOLERANCE; Hot Temperature; hyperthermophile; immobilized enzyme; IMMOBILIZED ENZYMES; MALATE DEHYDROGENASE; Malate Dehydrogenase - chemistry; Malate Dehydrogenase - metabolism; MALATE DESHYDROGENASE; MALATO DESHIDROGENASA; MICRO-ORGANISME THERMOPHILE; MICROORGANISMOS TERMOFILOS; Protein Engineering - methods; Recombinant Proteins - chemistry; Recombinant Proteins - metabolism; Temperature; Thermococcus - genetics; THERMOPHILIC MICROORGANISMS; TOLERANCE A LA CHALEUR; TOLERANCIA AL CALOR; UREASA; UREASE; Urease - chemistry; Urease - metabolism; immobilized enzyme; heat stabilization; chaperonin; hyperthermophile; archaea; Heat; Archaeobacteria; Hyperthermophily; Stabilization; Bacteria; Immobilized enzyme
• ISSN: 1389-1723; 1347-4421
• DOI: 10.1263/jbb.101.131

Chaperonins suppress the denaturation of proteins and promote protein folding in vivo. Because hyperthermophilic chaperonins are expected to be used as a stabilizer for proteins, the effects of a group II chaperonin from a hyperthermophilic archaeum, Thermococcus strain KS-1 ( T. KS-1 cpn), on the stabilization of mesophilic and thermophilic free enzymes and an enzyme co-immobilized with T. KS-1 cpn were studied. T. KS-1 cpn prevented the thermal inactivation of yeast alcohol dehydrogenase (ADH), jack bean urease, and Thermus flavus malate dehydrogenase (MDH) at high temperatures. T. KS-1 cpn also improved the long-term stability of ADH at lower temperatures. Moreover, the residual ADH activity of ADH co-entrapped with T. KS-1 cpn was improved and maintained at a higher level than that of the entrapped ADH without chaperonin. T. KS-1 cpn is useful for the stabilization of free and immobilized enzymes and applicable to various fields of biotechnology.