Dataset Information

PH Dependence of Chitosan Enzymolysis.

ABSTRACT: As a means of making chitosan more useful in biotechnological applications, it was hydrolyzed using pepsin, chitosanase and ?-amylase. The enzymolysis behavior of these enzymes was further systematically studied for its effectiveness in the production of low-molecular-weight chitosans (LMWCs) and other derivatives. The study showed that these enzymes depend on ion hydronium (H3O+), thus on pH with a pH dependence fitting R2 value of 0.99. In y = 1.484[H^+] + 0.114, the equation of pH dependence, when [H^+] increases by one, y (k_0/k_m) increases by 1.484. From the temperature dependence study, the activation energy (Ea) and pre-exponential factor (A) were almost identical for two of the enzymes, but a considerable difference was observed in comparison with the third enzyme. Chitosanase and pepsin had nearly identical Ea, but ?-amylase was significantly lower. This serves as evidence that the hydrolysis reaction of ?-amylase relies on low-barrier hydrogen bonds (LBHBs), which explains its low Ea in actual conditions. The confirmation of this phenomenon was further derived from a similarly considerable difference in the order magnitudes of A between ?-amylase and the other two enzymes, which was more than five. Variation of the rate constants of the enzymatic hydrolysis of chitosan with temperature follows the Arrhenius equation.

SUBMITTER: Gohi BFCA

PROVIDER: S-EPMC6432485 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

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pH Dependence of Chitosan Enzymolysis.

Gohi Bi Foua Claude Alain BFCA Zeng Hong-Yan HY Pan A Dan AD Han Jing J Yuan Jian J

Polymers 20170513 5

As a means of making chitosan more useful in biotechnological applications, it was hydrolyzed using pepsin, chitosanase and α-amylase. The enzymolysis behavior of these enzymes was further systematically studied for its effectiveness in the production of low-molecular-weight chitosans (LMWCs) and other derivatives. The study showed that these enzymes depend on ion hydronium (H3O+), thus on pH with a pH dependence fitting R2 value of 0.99. In y = 1.484[H^+] + 0.114, the equation of pH dependence, ...[more]

PMID: 30970852

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Project description:The increasing use of methacrylate-based materials in tissue engineering and dental restorations demands detailed evaluation of enzymolysis of these materials due to toxicity, durability, and biocompatibility concerns. The objective of this study is to develop tools for assessing and ranking the enzymolysis kinetics of dimethacrylate (DMA) compounds. Triethyleneglycol DMA and diurethane DMA are employed as model DMAs for kinetic studies of 2-step enzymolysis by 2 esterases, pseudocholine esterase and cholesterol esterase. In addition, the intermediate hydrolysis products, mono-methacrylates (mono-MAs), are prepared via esterases. The kinetics of DMA enzymolysis are evaluated per the concentrations of DMA. The enzymolysis products are quantified by high-performance liquid chromatography. Additionally, stoichiometric analysis and a Berkeley Madonna model are employed to compare the efficacy of esterases in DMA enzymolysis. The chemical structure of mono-MAs is verified by proton and heteronuclear single quantum coherence (2D 1H-13C) nuclear magnetic resonance spectroscopy and mass spectrometry. In evaluating the ratio of sequential and simultaneous degradations of DMA and mono-MA, the stoichiometric analysis draws the same conclusions without using [mono-MA] as the experimental observation using [mono-MA]. The majority of the 4 esterase-DMA combinations undergo the sequential enzyme-catalyzed hydrolysis, from DMA to mono-MA to diol. However, cholesterol esterase is more effective than pseudocholine esterase in maintaining sequential degradation until >90% of DMA is decomposed. Both enzymolysis steps are first-order reactions. The mono-MAs are more hydrolysis resistant than DMAs. Moreover, esterase efficacy and selectivity on DMA enzymolysis are presented. The stoichiometric analysis provides valuable tools in assessing DMA enzymolysis when mono-MA is difficult to be obtained. The resistance of mono-MAs to enzymolysis suggests a need for thorough toxicity evaluations of these intermediate compounds. It also advocates the alternative approaches in designing and developing durable and biocompatible materials.

Dataset Information

PH Dependence of Chitosan Enzymolysis.

Publications

pH Dependence of Chitosan Enzymolysis.

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