Evidence map›Paper›PMID 15362976›Full record

ArticleThe Biochemical journal2005

Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy.

Antonino Natalello, Diletta Ami, Stefania Brocca, Marina Lotti, Silvia M Doglia

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Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

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23citing papers in PubMed
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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

23 citing papers in PubMed.

  1. Article
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  5. Enzyme-Support Interactions ofACS applied materials & interfaces · 2025
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  12. Article
  13. Article
  14. Article
  15. Frozen Microemulsions for MAPLE Immobilization of Lipase.Molecules (Basel, Switzerland) · 2017
    Article
  16. Article
  17. Article
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  19. Article
  20. Article
4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Antonino NatalelloDipartimento di Biotecnologie e Bioscienze, Università degli Studi di Milano-Bicocca, Piazza della Scienza 2, 20126 Milano, Italy.
Diletta Ami
Stefania Brocca
Marina Lotti
Silvia M Doglia

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The secondary structure of lipase 1 from Candida rugosa, a model system for large monomeric enzymes, has been studied by FTIR (Fourier-transform infrared) spectroscopy in water and 2H2O. The secondary structure content, determined by the analysis of the amide I band absorption through second derivative and curve fitting procedures, is in agreement with that estimated by X-ray data and predicts, in addition, the existence of two classes of alpha-helices. We have also investigated the enzyme stability and aggregation at high temperature by following the protein unfolding. The thermal stability determined by FTIR is in excellent agreement with the temperature dependence of the lipase activity. Furthermore, new insights on the glycosylation of the recombinant protein produced in Pichia pastoris and on its heterogeneity related to different fermentation batches were obtained by the analysis of the IR absorption in the 1200-900 cm(-1) carbohydrate region. A drastic reduction of the intensity of this band was found after enzymic deglycosylation of the protein. To confirm that the FTIR absorption in the 1200-900 cm(-1) region depends on the carbohydrate content and glycoform distribution, we performed an MS analysis of the protein sugar moieties. Glycosidic structures of the high mannose type were found, with mannoses ranging from 8 to 25 residues.

Indexed as

AmidesCandidaCarboxylic Ester HydrolasesFungal ProteinsGlycosylationHot TemperatureLipaseProtein ConformationProtein DenaturationProtein FoldingProtein Structure, SecondarySolutionsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSpectroscopy, Fourier Transform InfraredAmidesCarboxylic Ester HydrolasesFungal ProteinsLipaseSolutions

Identifiers

PMID15362976
PMCPMC1134723

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.