C. G. Boeriu

Publications

3 Structural Analysis of Lignins from Different Sources

Authors: F. Peter, I. F. Fiţigău, C. G. Boeriu

Abstract:

Five lignin samples were fractionated with Acetone/Water mixtures and the obtained fractions were subjected to extensive structural characterization, including Fourier Transform Infrared (FT-IR), Gel permeation Chromatography (GPC) and Phosphorus-31 NMR spectroscopy (31P-NMR). The results showed that for all studied lignins the solubility increases with the increment of the acetone concentration. Wheat straw lignin has the highest solubility in 90/10 (v/v) Acetone/Water mixture, 400 mg lignin being dissolved in 1 mL mixture. The weight average molecular weight of the obtained fractions increased with the increment of acetone concentration and thus with solubility. 31P-NMR analysis based on lignin modification by reactive phospholane into phosphitylated compounds was used to differentiate and quantify the different types of OH groups (aromatic, aliphatic, and carboxylic) found in the fractions obtained with 70/30 (v/v) Acetone/Water mixture.

Keywords: Fractionation, Lignin, GPC, FT-IR

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2 Synthesis of Peptide Amides using Sol-Gel Immobilized Alcalase in Batch and Continuous Reaction System

Authors: F. Peter, C. G. Boeriu, L. N. Corîci, A. E. Frissen, D -J. Van Zoelen, I. F. Eggen, C. M. Davidescu

Abstract:

Two commercial proteases from Bacillus licheniformis (Alcalase 2.4 L FG and Alcalase 2.5 L, Type DX) were screened for the production of Z-Ala-Phe-NH2 in batch reaction. Alcalase 2.4 L FG was the most efficient enzyme for the C-terminal amidation of Z-Ala-Phe-OMe using ammonium carbamate as ammonium source. Immobilization of protease has been achieved by the sol-gel method, using dimethyldimethoxysilane (DMDMOS) and tetramethoxysilane (TMOS) as precursors (unpublished results). In batch production, about 95% of Z-Ala-Phe-NH2 was obtained at 30°C after 24 hours of incubation. Reproducibility of different batches of commercial Alcalase 2.4 L FG preparations was also investigated by evaluating the amidation activity and the entrapment yields in the case of immobilization. A packed-bed reactor (0.68 cm ID, 15.0 cm long) was operated successfully for the continuous synthesis of peptide amides. The immobilized enzyme retained the initial activity over 10 cycles of repeated use in continuous reactor at ambient temperature. At 0.75 mL/min flow rate of the substrate mixture, the total conversion of Z-Ala-Phe-OMe was achieved after 5 hours of substrate recycling. The product contained about 90% peptide amide and 10% hydrolysis byproduct.

Keywords: protease, packed-bed reactor, peptide amide, sol-gel immobilization

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1 Lipase Catalyzed Synthesis of Aromatic Esters of Sugar Alcohols

Authors: R. Croitoru, F. Peter, C. G. Boeriu, A. E. Frissen, C. M. Davidescu, L. A. M. van den Broek

Abstract:

Commercially available lipases (Candida antarctica lipase B, Novozyme 435, Thermomyces lanuginosus lipase, and Lipozyme TL IM), as well as sol-gel immobilized lipases, have been screened for their ability to acylate regioselectively xylitol, sorbitol, and mannitol with a phenolic ester in a binary mixture of t-butanol and dimethylsulfoxide. HPLC and MALDI-TOF MS analysis revealed the exclusive formation of monoesters for all studied sugar alcohols. The lipases immobilized by the sol-gel entrapment method proved to be efficient catalysts, leading to high conversions (up to 60%) in the investigated acylation reactions. From a sequence of silane precursors with different nonhydrolyzable groups in their structure, the presence of octyl and i-butyl group was most beneficial for the catalytic activity of sol-gel entrapped lipases in the studied process.

Keywords: transesterification, specificity, lipase, phenolic ester, sugar alcohol

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