Physicochemical properties of gelatin gels from walleye pollock (Theragra chalcogramma) skin cross-linked by gallic acid and rutin

Yan, Mingyan; Li, Bafang; Zhao, Xue; Yi, Junyao

doi:10.1016/j.foodhyd.2010.08.019

Cited by 99 publications

(44 citation statements)

References 30 publications

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“…Therefore, a basic laboratory ink formulation was prepared that uses gallic acid as a potential ligand to iron. Binding of gallic acid to parchment collagen is much weaker by comparison to that of a tannin [60,[62][63][64].…”

Section: Experimental Designmentioning

confidence: 94%

A study of the deterioration of aged parchment marked with laboratory iron gall inks using FTIR-ATR spectroscopy and micro hot table

2016

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A great number of historic manuscripts, drawings, etc., many of which are stored and/or exhibited in museums, archives and various collections contain iron gall inks (IGIs) as base scripting material. Although the severe deterioration effect of IGIs on paper has been recognized and its chemistry has been explored, little focus has been given on IGIs on parchment. A study was designed to investigate laboratory iron gall inks containing ferrous sulphate and gallic acid (LIG formulation) and with added quantities of gum arabic (LIGG formulation). Specimens marked with the above ink types were artificially aged at 80 °C and 80 % RH for up to 32 days. Micro hot table (MHT) thermal analysis showed a decrease in the shrinkage temperatures in inked areas of aged parchment of up to 15.5 °C. Results of FTIR-ATR spectroscopy showed intense migration of sulphate ions from inked spots to neighbouring ink-free areas at the surface of parchment in both ink formulations, also confirmed by SEM microanalysis results. This effect peaked at short-moderate times of artificial ageing, where calcium sulphate was identified and located at the surface of ink-free areas. Moreover, early signs for gelatinization of collagen also resulted from analysis of Amide I and II infrared bands, where the random coil content increased upon ageing as compared to the helical one.

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Section: Experimental Designmentioning

confidence: 94%

A study of the deterioration of aged parchment marked with laboratory iron gall inks using FTIR-ATR spectroscopy and micro hot table

2016

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“…Some of the specific points are as following-1. Type I collagen prepared by the hot-water method, authors stated that the extraction the collagen were performed as previously described by Yan et al (2011) with slight modifications. However, Yan et al 2011 did not describe any method for collagen extraction process.…”

Section: Technical Comments On Published Articles On Collagen Extractionmentioning

confidence: 99%

Technical note on the isolation and characterization of collagen from fish waste material

Kumar

Rani

2017

J Food Sci Technol

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The aim of this manuscript was to evaluate the major technical problems on the isolation and characterization of the collagen from fish waste materials that were usually faced by the growing researchers. Although the original research article published by authors contributed new information to the literature, some of them were failed to provide sufficient details in order to reproduce the study as well as could not adequately interpret/compared the results with other publications. Therefore, it is required to research the technical problems during the isolation and characterization of the collagen. This technical note provides the information which is crucial for the reader's and growing researchers for understanding as an essential part of the published research studies about the collagen extraction and characterization. Hence, this technical note may be helpful to those working on the collagen extraction and characterization from fish/marine waste materials.

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“…Caffeic acid (C 9 H 8 O 4 ) has antioxidant, antitumor and anti-inflammatory properties (Jiang et al, 2005). Rutin (C 27 H 30 O 16 ) is a glycosylated form of quercetin (30, 40-dihydroxyflavonol) (Yan et al, 2011). Phenolic compounds as 3% caffeic acid can be used to improve the mechanical properties of PPP film (Nuthong et al, 2009b).…”

Section: Introductionmentioning

confidence: 99%

Modification and characterisation of porcine plasma protein with natural agents as potential cross‐linkers

Samsalee

Sothornvit

2017

Int J of Food Sci Tech

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Summary Modification of porcine plasma protein (PPP) using the natural cross‐linkers at different concentrations of rutin (0.6–1% w/w), caffeic acid (1–3% w/w) and genipin (0.15–0.5% w/w) on chemical and thermal properties of PPP was investigated. Among these, rutin was the most significant effective natural agent corresponding to a decrease in the free amino group and sulphydryl group contents including a change in the protein bands’ intensity from SDS‐PAGE. However, genipin exhibited greater thermal properties of modified PPP. Moreover, the modification affected the colour of PPP and a change in the FT‐IR spectra of the samples. The suitable concentrations of each natural agent were 0.6% rutin, 0.5% genipin and 3% caffeic acid. Therefore, natural cross‐linkers such as rutin, caffeic acid and genipin can be considered as alternative cross‐linkers to improve the properties of PPP for food processing and biopolymer material applications as they are nontoxic.

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Physicochemical properties of gelatin gels from walleye pollock (Theragra chalcogramma) skin cross-linked by gallic acid and rutin

Cited by 99 publications

References 30 publications

A study of the deterioration of aged parchment marked with laboratory iron gall inks using FTIR-ATR spectroscopy and micro hot table

A study of the deterioration of aged parchment marked with laboratory iron gall inks using FTIR-ATR spectroscopy and micro hot table

Technical note on the isolation and characterization of collagen from fish waste material

Modification and characterisation of porcine plasma protein with natural agents as potential cross‐linkers

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