Literature DB >> 12527275

A natural compound (reuterin) produced by Lactobacillus reuteri for biological-tissue fixation.

Hsing-Wen Sung1, Chiun-Nan Chen, Hsiang-Fa Liang, Min-Hao Hong.   

Abstract

The study was undertaken to examine the degree of tissue fixation by reuterin, a natural compound produced by Lactobacillus reuteri, at distinct fixation conditions (pH, temperature, and fixative concentration). Additionally, the rate of tissue fixation by reuterin was investigated using glutaraldehyde as a control. It was found by the Fourier transformed infrared spectroscopy and nuclear magnetic resonance spectroscopy that both mono- and di-aldehyde reuterin oligomers may be present in the acidic and basic aqueous reuterin solutions. Therefore, reuterin may crosslink biological tissues as glutaraldehyde (a di-aldehyde agent). The degree of tissue fixation by reuterin is significantly affected by its fixation conditions. Generally, with increasing the pH, temperature, or fixative concentration, the reduction in free-amino-group content, denaturation temperature, tensile strength, and resistance against enzymatic degradation of the reuterin-fixed tissue increased significantly. Also, the rate of tissue fixation by reuterin is significantly slower than that by glutaraldehyde. However, after fixation, it was noted that the reuterin-fixed tissue has comparable free-amino-group content, denaturation temperature, tensile strength, and resistance against enzymatic degradation as the glutaraldehyde-fixed tissue. Copyright 2002 Elsevier Science Ltd.

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Year:  2003        PMID: 12527275     DOI: 10.1016/s0142-9612(02)00509-4

Source DB:  PubMed          Journal:  Biomaterials        ISSN: 0142-9612            Impact factor:   12.479


  6 in total

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Authors:  Bettina Hoffmann; Elias Volkmer; Andreas Kokott; Peter Augat; Michael Ohnmacht; Nicole Sedlmayr; Matthias Schieker; Lutz Claes; Wolf Mutschler; Günter Ziegler
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5.  Acrolein contributes strongly to antimicrobial and heterocyclic amine transformation activities of reuterin.

Authors:  Christina Engels; Clarissa Schwab; Jianbo Zhang; Marc J A Stevens; Corinne Bieri; Marc-Olivier Ebert; Kristopher McNeill; Shana J Sturla; Christophe Lacroix
Journal:  Sci Rep       Date:  2016-11-07       Impact factor: 4.379

6.  Polymorphisms in the human tropoelastin gene modify in vitro self-assembly and mechanical properties of elastin-like polypeptides.

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  6 in total

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