The modification of the triple helical structure of gelatin in aqueous solution 3. The influence of cationic surfactants

Wüstneck, R.; Buder, E.; Wetzel, R.; Hermel, H.

doi:10.1007/bf01410188

Cited by 32 publications

(8 citation statements)

References 12 publications

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“…The triple helical structure of the gelatin is strongly decreased in acidic environments [1], but it is extremely decreased by adding surfactants which leads to the appearance of the 222 nm peak in the negative part of the graph for CTAB. Furthermore, this result shows that in acidic environment the influence of the nonionic surfactant on the triple helical structure of the gelatin is strong in comparison to that found for pH = 7.0, which supports our assumption of [2]. In the case of SDS the formation of fl-sheets was found characterized by similar CD-spectra [11,12].…”

Section: Methodssupporting

confidence: 86%

The modification of the triple helical structure of gelatin in aqueous solution 3. The influence of nonionic surfactants

Wstneck¹,

Buder

Wetzel

et al. 1989

Colloid & Polymer Sci

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Using CD-measurements the influence of nonionic surfactants (dodecyl polyoxyethylene, ethoxylated para tert. octyl phenol, commercial nonionic WON 100 and octyl diethyl phosphinoxid) on the secondary structure of gelatin in aqueous solutions was investigated. At surfactant concentrations smaller than the c.m.c, the triple helical content of the gelatin is increased. At concentrations exceeding the c.m.c, the triple helical content decreases. Chain reversals of the peptide chains after the destruction of the triple helical structure were shown to appear in acidic environment at 298 K. This destruction is reversible by rechilling the solution.

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Section: Methodssupporting

confidence: 86%

The modification of the triple helical structure of gelatin in aqueous solution 3. The influence of nonionic surfactants

Wstneck¹,

Buder

Wetzel

et al. 1989

Colloid & Polymer Sci

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“…But reports on the interaction of gelatin with non-ionic surfactants 43 or with cationic surfactants of varied types have been strikingly limited. [44][45][46][47][48] We have studied here the interaction of gelatin with the alkyltrimethylammonium bromide surfactants, and in particular the analogues of the C 16 variety having modified head groups in detail. The surface and bulk properties have been examined by various techniques and a schematic illustration of the involved interaction processes has been proposed.…”

Section: Introductionmentioning

confidence: 99%

Physicochemistry of hexadecylammonium bromide and its methyl and ethanolic head group analogues in buffered aqueous and gelatin solution

Mitra

Moulik

2010

J Chem Sci

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In this work, the interfacial and bulk behaviour of the amphiphiles hexadecylammonium bromide and its methyl and ethanolic head group analogues in buffered aqueous and gelatin solution has been examined. The analogues are of two categories: the methyl and the combined methyl and ethanolic head group representatives are considered as Group A compounds, and all non-methyl but ethanolic head group species are taken as Group B compounds. Different physical techniques have been employed to ascertain the amphiphilic behaviour in solution. The self-aggregation of these surfactants at different pH has been studied along with pH dependent interfacial activity of gelatin. The interaction of the two categories of the surfactants with gelatin at different pH has been investigated. A scheme for this interaction at various stages of the process has been proposed. The influence of the surfactant head groups on the interaction process has been assessed.

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“…Myoglobin (Mb), having molecular dimensions of 4.5 × 3.5 × 2.5 nm (Wüstneck et al, 1989), is a heme protein that originally functions as oxygen storage and transportation. Mb can be transformed into peroxidase by protein engineering, which can catalyze various reactions such as oxidation of guaiacol and indole (Xu et al, 2012;Liao et al, 2020) and decolorization of industrial dyes (Zhang et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Effects of Pore Size and Crosslinking Methods on the Immobilization of Myoglobin in SBA-15

Miao

Sun

et al. 2022

Front. Bioeng. Biotechnol.

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A series of stable mesoporous silica sieves (SBA-15) with different pore sizes (9.8, 7.2, and 5.5 nm) were synthesized using a hydrothermal method. The resulting mesoporous material was then utilized for protein immobilization using myoglobin (Mb) as the target protein. The effects of pore size and adsorption methods on the immobilization efficiency of Mb in a mesoporous material were studied. The SBA-15 with a pore size of 7.2 nm showed the best loading capacity, reaching 413.8 mg/g. The SBA-15 with a pore size of 9.8 nm showed the highest retained catalytic ability (92.36%). The immobilized enzyme was more stable than the free enzyme. After seven consecutive assay cycles, Mb adsorbed by SBA-15 (Mb/SBA-15) and Mb adsorbed by SBA-15 and crosslinked with glutaraldehyde (Mb/G/SBA-15) retained 36.41% and 62.37% of their initial activity, respectively.

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The modification of the triple helical structure of gelatin in aqueous solution 3. The influence of cationic surfactants

Cited by 32 publications

References 12 publications

The modification of the triple helical structure of gelatin in aqueous solution 3. The influence of nonionic surfactants

The modification of the triple helical structure of gelatin in aqueous solution 3. The influence of nonionic surfactants

Physicochemistry of hexadecylammonium bromide and its methyl and ethanolic head group analogues in buffered aqueous and gelatin solution

Effects of Pore Size and Crosslinking Methods on the Immobilization of Myoglobin in SBA-15

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