Investigation of endoglucanase selectivity on carboxymethyl cellulose by mass spectrometric techniques

Jonas Enebro, Dane Momcilovic (Corresponding Author), Matti Siika-aho, Sigbritt Karlsson

Research output: Contribution to journalArticleScientificpeer-review

14 Citations (Scopus)

Abstract

The benefits of applying cellulose selective enzymes as analytical tools for chemical structure characterization of cellulose derivatives have been frequently addressed over the years. In a recent study the high selectivity of cellulase Cel45A from Trichoderma reesei (Tr Cel45A) was utilized for relating the chemical structure to the flow properties of carboxymethyl cellulose (CMC). However, in order to take full advantage of the enzymatic hydrolysis the enzyme selectivity on the cellulose substrate must be further investigated. Therefore, the selectivity of Tr Cel45A on CMC was studied by chemical sample preparation of the enzyme products followed by mass spectrometric chemical structure characterization. The results strongly suggest that, in accordance with recent studies, also this highly selective endoglucanase is able to catalyze hydrolysis of glucosidic bonds adjacent to mono-substituted anhydroglucose units (AGUs). Furthermore, the results also indicate that substituents on the nearby AGUs will affect the hydrolysis.
Original languageEnglish
Pages (from-to)271-280
Number of pages10
JournalCellulose
Volume16
Issue number2
DOIs
Publication statusPublished - 2009
MoE publication typeA1 Journal article-refereed

Keywords

  • Carboxymethyl cellulose
  • Selective hydrolysis
  • Cellulase
  • Permethylation
  • MALDI
  • ESI
  • Mass spectrometry

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