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Structural differences of commercial and recombinant lipase B from Candida antarctica: An important implication on enzymes thermostability.

التفاصيل البيبلوغرافية
العنوان: Structural differences of commercial and recombinant lipase B from Candida antarctica: An important implication on enzymes thermostability.
المؤلفون: Brito E Cunha DA; Laboratório de Bioquímica Estrutural de Proteínas, Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil., Bartkevihi L; Laboratório de Bioquímica Estrutural de Proteínas, Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil., Robert JM; Laboratório de Biotecnologia Microbiana, Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil., Cipolatti EP; Laboratório de Biotecnologia Microbiana, Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil., Ferreira ATS; Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz, Rio de Janeiro 21040-900, Brazil., Oliveira DMP; Laboratório de Bioquímica Estrutural de Proteínas, Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil., Gomes-Neto F; Laboratório de Toxinologia, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz, Rio de Janeiro 21040-900, Brazil., Almeida RV; Laboratório de Microbiologia Molecular e Proteínas, Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil., Fernandez-Lafuente R; Departamento de Biocatálisis. ICP-CSIC, Campus UAM-CSIC, Madrid, Spain., Freire DMG; Laboratório de Biotecnologia Microbiana, Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil. Electronic address: freire@iq.ufrj.br., Anobom CD; Laboratório de Bioquímica Estrutural de Proteínas, Departamento de Bioquímica, Instituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941-909, Brazil. Electronic address: anobom@iq.ufrj.br.
المصدر: International journal of biological macromolecules [Int J Biol Macromol] 2019 Nov 01; Vol. 140, pp. 761-770. Date of Electronic Publication: 2019 Aug 18.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier
Original Publication: Guildford, Eng., IPC Science and Technology Press.
مواضيع طبية MeSH: Recombinant Fusion Proteins*, Candida/*enzymology , Fungal Proteins/*chemistry , Lipase/*chemistry, Amino Acid Sequence ; Candida/genetics ; Enzyme Activation ; Enzyme Stability ; Fungal Proteins/genetics ; Fungal Proteins/isolation & purification ; Fungal Proteins/metabolism ; Hydrolysis ; Lipase/genetics ; Lipase/isolation & purification ; Lipase/metabolism ; Models, Molecular ; Protein Conformation ; Structure-Activity Relationship ; Temperature ; Thermodynamics
مستخلص: Lipase B from Candida antarctica (CalB) is the most widely used lipase, including in many industrial sectors, such as in biodiesel and pharmaceuticals production. CalB has been produced by heterologous expression using Pichia pastoris under PGK constitutive promoter (named LipB). Here, we have studied the structural features of commercial CalB and LipB enzymes using circular dichroism and fluorescence under different conditions. In the presence of denaturing agents CalB was more stable than LipB, in contrast, at increasing temperatures, LipB was more thermostable than CalB. Mass spectrometry data indicates that both enzymes have an insertion of amino acids related to α-factor yeast signal, however LipB enzyme showed the addition of nine residues at the N-terminal while CalB showed only four residues. Molecular modeling of LipB showed the formation of an amphipathic α-helix in N-terminal region that was not observed in CalB. This data suggests that this new α-helix possess could be involved in LipB thermostability. These results associated with new structural studies may provide information to the design of novel biocatalysts.
(Copyright © 2019 Elsevier B.V. All rights reserved.)
المشرفين على المادة: 0 (Fungal Proteins)
0 (Recombinant Fusion Proteins)
EC 3.1.1.3 (Lipase)
EC 3.1.1.3 (lipase B, Candida antarctica)
تواريخ الأحداث: Date Created: 20190822 Date Completed: 20200415 Latest Revision: 20200415
رمز التحديث: 20240628
DOI: 10.1016/j.ijbiomac.2019.08.148
PMID: 31434004
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-0003
DOI:10.1016/j.ijbiomac.2019.08.148