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Analysis of institutional authors

Remacha MAuthorFernandez-Lobato MAuthor

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March 26, 2018
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Article

Use of chitin and chitosan to produce new chitooligosaccharides by chitinase Chit42: enzymatic activity and structural basis of protein specificity.

Publicated to:Microbial Cell Factories. 17 (1): 47-47 - 2018-03-22 17(1), DOI: 10.1186/s12934-018-0895-x

Authors: Elias Kidibule, Peter; Santos-Moriano, Paloma; Jimenez-Ortega, Elena; Ramirez-Escudero, Mercedes; Carmen Limon, M; Remacha, Miguel; Jose Plou, Francisco; Sanz-Aparicio, Julia; Fernandez-Lobato, Maria

Affiliations

;Department of Crystallography and Structural Biology, Institute of Physical Chemistry Rocasolano (CSIC), C/ Serrano, 119, 28006, Madrid, Spain - Author
;Department of Genetic, University of Sevilla, Avenida Reina Mercedes s/n, 41012, Seville, Spain - Author
;Department of Molecular Biology, Centre for Molecular Biology Severo Ochoa (CSIC-UAM), University Autonomous from Madrid, C/ Nicolás Cabrera, 1, Cantoblanco, 28049, Madrid, Spain - Author
;Institute of Catalysis and Petrochemistry, CSIC, C/ Marie Curie, 2, Cantoblanco, 28049, Madrid, Spain - Author
CSIC - Author
CSIC, Inst Catalysis & Petrochem, C Marie Curie 2, Madrid 28049, Spain - Author
Department of Molecular Biology, Centre for Molecular Biology Severo Ochoa (CSIC-UAM), University Autonomous from Madrid, C/ Nicolás Cabrera, 1, Cantoblanco, 28049, Madrid, Spain - Author
Inst Phys Chem Rocasolano CSIC, Dept Crystallog & Struct Biol, C Serrano 119, Madrid 28006, Spain - Author
Univ Autonomous Madrid, Ctr Mol Biol Severo Ochoa CSIC UAM, Dept Mol Biol, C Nicolas Cabrera 1, Madrid 28049, Spain - Author
Univ Seville, Dept Genet, Ave Reina Mercedes S-N, E-41012 Seville, Spain - Author
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Abstract

Chitinases are ubiquitous enzymes that have gained a recent biotechnological attention due to their ability to transform biological waste from chitin into valued chito-oligomers with wide agricultural, industrial or medical applications. The biological activity of these molecules is related to their size and acetylation degree. Chitinase Chit42 from Trichoderma harzianum hydrolyses chitin oligomers with a minimal of three N-acetyl-D-glucosamine (GlcNAc) units. Gene chit42 was previously characterized, and according to its sequence, the encoded protein included in the structural Glycoside Hydrolase family GH18.Chit42 was expressed in Pichia pastoris using fed-batch fermentation to about 3 g/L. Protein heterologously expressed showed similar biochemical properties to those expressed by the natural producer (42 kDa, optima pH 5.5-6.5 and 30-40 °C). In addition to hydrolyse colloidal chitin, this enzyme released reducing sugars from commercial chitosan of different sizes and acetylation degrees. Chit42 hydrolysed colloidal chitin at least 10-times more efficiently (defined by the kcat/Km ratio) than any of the assayed chitosan. Production of partially acetylated chitooligosaccharides was confirmed in reaction mixtures using HPAEC-PAD chromatography and mass spectrometry. Masses corresponding to (D-glucosamine)1-8-GlcNAc were identified from the hydrolysis of different substrates. Crystals from Chit42 were grown and the 3D structure determined at 1.8 Å resolution, showing the expected folding described for other GH18 chitinases, and a characteristic groove shaped substrate-binding site, able to accommodate at least six sugar units. Detailed structural analysis allows depicting the features of the Chit42 specificity, and explains the chemical nature of the partially acetylated molecules obtained from analysed substrates.Chitinase Chit42 was expressed in a heterologous system to levels never before achieved. The enzyme produced small partially acetylated chitooligosaccharides, which have enormous biotechnological potential in medicine and food. Chit42 3D structure was characterized and analysed. Production and understanding of how the enzymes generating bioactive chito-oligomers work is essential for their biotechnological application, and paves the way for future work to take advantage of chitinolytic activities.

Keywords

Chit42 3d structureChitinaseChitooligosaccharidesPartially acetylated chitooligosaccharidesTrichoderma harzianum

Quality index

Bibliometric impact. Analysis of the contribution and dissemination channel

The work has been published in the journal Microbial Cell Factories due to its progression and the good impact it has achieved in recent years, according to the agency WoS (JCR), it has become a reference in its field. In the year of publication of the work, 2018, it was in position 28/161, thus managing to position itself as a Q1 (Primer Cuartil), in the category Biotechnology & Applied Microbiology.

From a relative perspective, and based on the normalized impact indicator calculated from World Citations provided by WoS (ESI, Clarivate), it yields a value for the citation normalization relative to the expected citation rate of: 2.38. This indicates that, compared to works in the same discipline and in the same year of publication, it ranks as a work cited above average. (source consulted: ESI Nov 14, 2024)

This information is reinforced by other indicators of the same type, which, although dynamic over time and dependent on the set of average global citations at the time of their calculation, consistently position the work at some point among the top 50% most cited in its field:

  • Weighted Average of Normalized Impact by the Scopus agency: 2.91 (source consulted: FECYT Feb 2024)
  • Field Citation Ratio (FCR) from Dimensions: 6.22 (source consulted: Dimensions Jul 2025)

Specifically, and according to different indexing agencies, this work has accumulated citations as of 2025-07-22, the following number of citations:

  • WoS: 58
  • Scopus: 69
  • Europe PMC: 25

Impact and social visibility

From the perspective of influence or social adoption, and based on metrics associated with mentions and interactions provided by agencies specializing in calculating the so-called "Alternative or Social Metrics," we can highlight as of 2025-07-22:

  • The use, from an academic perspective evidenced by the Altmetric agency indicator referring to aggregations made by the personal bibliographic manager Mendeley, gives us a total of: 103.
  • The use of this contribution in bookmarks, code forks, additions to favorite lists for recurrent reading, as well as general views, indicates that someone is using the publication as a basis for their current work. This may be a notable indicator of future more formal and academic citations. This claim is supported by the result of the "Capture" indicator, which yields a total of: 108 (PlumX).

With a more dissemination-oriented intent and targeting more general audiences, we can observe other more global scores such as:

  • The Total Score from Altmetric: 0.75.
  • The number of mentions on the social network X (formerly Twitter): 2 (Altmetric).

It is essential to present evidence supporting full alignment with institutional principles and guidelines on Open Science and the Conservation and Dissemination of Intellectual Heritage. A clear example of this is:

  • The work has been submitted to a journal whose editorial policy allows open Open Access publication.

Leadership analysis of institutional authors

There is a significant leadership presence as some of the institution’s authors appear as the first or last signer, detailed as follows: Last Author (FERNANDEZ LOBATO, MARIA).