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Microorganisms 2018, 6(4), 108; https://doi.org/10.3390/microorganisms6040108

Contribution of the Oligomeric State to the Thermostability of Isoenzyme 3 from Candida rugosa

Department of Food and Analytical Chemistry, Sciences Faculty of Ourense, University of Vigo, As Lagoas s/n, 32004 Ourense, Spain
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Received: 14 September 2018 / Revised: 15 October 2018 / Accepted: 16 October 2018 / Published: 19 October 2018
(This article belongs to the Special Issue Thermophiles and Thermozymes)
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Abstract

Thermophilic proteins have evolved different strategies to maintain structure and function at high temperatures; they have large, hydrophobic cores, and feature increased electrostatic interactions, with disulfide bonds, salt-bridging, and surface charges. Oligomerization is also recognized as a mechanism for protein stabilization to confer a thermophilic adaptation. Mesophilic proteins are less thermostable than their thermophilic homologs, but oligomerization plays an important role in biological processes on a wide variety of mesophilic enzymes, including thermostabilization. The mesophilic yeast Candida rugosa contains a complex family of highly related lipase isoenzymes. Lip3 has been purified and characterized in two oligomeric states, monomer (mLip3) and dimer (dLip3), and crystallized in a dimeric conformation, providing a perfect model for studying the effects of homodimerization on mesophilic enzymes. We studied kinetics and stability at different pHs and temperatures, using the response surface methodology to compare both forms. At the kinetic level, homodimerization expanded Lip3 specificity (serving as a better catalyst on soluble substrates). Indeed, dimerization increased its thermostability by more than 15 °C (maximum temperature for dLip3 was out of the experimental range; >50 °C), and increased the pH stability by nearly one pH unit, demonstrating that oligomerization is a viable strategy for the stabilization of mesophilic enzymes. View Full-Text
Keywords: Candida rugosa; lipase; kinetic; interfacial activation; inhibition; dimerization; structure Candida rugosa; lipase; kinetic; interfacial activation; inhibition; dimerization; structure
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Álvarez-Cao, M.-E.; González, R.; Pernas, M.A.; Rúa, M.L. Contribution of the Oligomeric State to the Thermostability of Isoenzyme 3 from Candida rugosa. Microorganisms 2018, 6, 108.

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