Model Studies on Chemical and Textural Modifications in Gelatin Films by Reaction with Glyoxal and Glycolaldehyde

Spanneberg, Robert; Osswald, Franziska; Kolesov, Igor; Anton, Werner; Radusch, Hans‐Joachim; Glomb, Marcus A.

doi:10.1021/jf9039827

Cited by 21 publications

(28 citation statements)

References 29 publications

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“…Another widely used dialdehyde is glyoxal. Similar results introduced by crosslinking with glyoxal were observed, such as a significant increase in strength and modulus of compression‐molded wheat gluten protein–based polymers at a relative humidity of 50%, an increase in water‐resistance properties and stiffness but a decrease in elongation of the wet‐cast gelatin biopolymer films, a decrease in the diameter of the electro‐spun zein fibers, and enhancement of the mechanical properties …”

Section: Crosslinkingsupporting

confidence: 75%

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Treatments of protein for biopolymer production in view of processability and physical properties: A review

Zhang

et al. 2016

J of Applied Polymer Sci

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The development of bio-based polymers from proteins has gained attention for their large availability and renewable and biodegradable nature. However, protein-based plastics have limited commercial applications because of several drawbacks, such as poor processability, brittleness, moisture sensitivity, and inferior mechanical and thermal properties. Extensive studies have been conducted to solve or ameliorate these issues by pretreatment or modification of proteins or protein-derived biopolymers before or during wet processing or dry processing at elevated temperatures. This review provides an overview of research efforts conducted in the area of physical and chemical treatment of proteins to achieve better processability, mechanical properties, and other physical performance based on a literature review in this subject. INTRODUCTIONBiopolymers derived from agricultural resources such as wool, cotton, leather, and silk have been extensively used by humans for a long time. Industrial use of agricultural commodities for fuels and consumer products began in the 1920s. They were soon replaced by petroleum-based chemicals after World War II because these synthetic polymers were cheaper, more durable, and more versatile. Advances in petroleum-based fuels and polymers have benefited mankind in numerous ways. However, sustainability of their production and use has become a societal concern. Besides, petroleum resources are finite, and their prices are likely to continue to rise in the future. The disposal of petroleum-based plastic has also been causing environmental concerns. 1 Since the early 1990s, the use of renewable biopolymers as a substitute for nonbiodegradable petrochemical-based polymers has again attracted considerable attention because of their environmental benefits such as renewability and biodegradability. Nowadays, natural polymers can even be tailored to meet specific needs.Protein is one of three main categories of renewable biopolymers aside from polysaccharides and polynucleotides that are derived from plant or animal resources. Plant proteins that can be used for bio-based plastics include soy protein, corn zein, wheat protein, cottonseed protein, and sunflower protein. Animal proteins such as blood meal, gelatin and collagen, keratin and feather quills, egg protein, whey protein, and meat and bone meal can also be used as a feedstock for such bio-based polymers. 2 Despite their environmental friendliness, proteinbased biopolymers have many shortcomings like lower mechanical properties when compared to petroleum-based polymers. 3 Due to the hydrogen bonds between C@O and NH groups, protein-based polymers have poor processability and exhibit high sensitivity to moisture. As a result, the protein-based polymers are very difficult to process without plasticizers or pretreatment. To date, overcoming these shortcomings of proteinbased bioplastics has proven difficult. Numerous methods have been investigated, including physical treatment, denaturation of the original protein in crystalline form, cleava...

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Section: Crosslinkingsupporting

confidence: 75%

“…For example, Spanneberg et al . reported that the mechanisms of protein modification by glyoxal and glycolaldehyde were different . Arginine was the major target to be modified by glyoxal, while glycolaldehyde reacted almost exclusively with lysine and other amino groups.…”

Section: Crosslinkingmentioning

confidence: 99%

Treatments of protein for biopolymer production in view of processability and physical properties: A review

Zhang

et al. 2016

J of Applied Polymer Sci

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“…Approximately 90% of the lysine modifications could not be accounted for. In addition, these authors showed that lysine was preferentially modified by GA as there was much less loss of arginine residues [31]. In our study, we did not analyze arginine because bLG contains only three arginine residues per molecule, whereas there are 16 lysine residues.…”

Section: Discussionmentioning

confidence: 86%

“…We did not analyze for other modifications as our analytical method is restricted to the detection and quantification of these modified amino acids [28]. Spanneberg et al [31] recently described the glycation of gelatin by GA. Similar to our findings, these authors detected only minor amounts of CML but no glyoxal-derived lysine dimer or imidazolinone.…”

Section: Discussionmentioning

confidence: 99%

Glycolaldehyde‐modified β‐lactoglobulin AGEs are unable to stimulate inflammatory signaling pathways in RAGE‐expressing human cell lines

Buetler

Latado

Leclerc

et al. 2010

Molecular Nutrition Food Res

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“…Glycolaldehyde was first identified as a fermentation inhibitor in our previous study (Jayakody et al 2011). Glycolaldehyde is formed by a retro-aldol condensation from sugars such as hexoses and pentoses during the treatment of cellulose and hemicellulose with hotcompressed water (Sasaki et al 2002;Kabyemela et al 1998;Sakaki et al 1996;Richards 1987). The toxicity of glycolaldehyde has been considered to be caused by its molecular feature of α-hydroxyaldehyde, which forms a Schiff base with the amino bases of proteins and is followed by an Amadori rearrangement, conversion to aldoamine, regeneration of a carbonyl base, and cross-linking of proteins (Acharya and Manning 1983) or formation of carboxymethyllysine and related advanced glycation end-products (Spanneberg et al 2010;Takeuchi et al 2000;Glomb and Monnier 1995). However, the mechanism of its toxicity, its detoxification mechanism, and its metabolic fate in a reductive environment have remained largely unknown.…”

Section: Introductionmentioning

confidence: 99%

Improvement of tolerance of Saccharomyces cerevisiae to hot-compressed water-treated cellulose by expression of ADH1

Jayakody

Horie

Hayashi

et al. 2012

Appl Microbiol Biotechnol

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Hot-compressed water treatment of cellulose and hemicellulose for subsequent bioethanol production is a novel, economically feasible, and nonhazardous method for recovering sugars. However, the hot-compressed water-treated cellulose and hemicellulose inhibit subsequent ethanol fermentation by the yeast Saccharomyces cerevisiae. To overcome this problem, we engineered a yeast strain with improved tolerance to hot-compressed water-treated cellulose. We first determined that glycolaldehyde has a greater inhibitory effect than 5-HMF and furfural and a combinational effect with them. On the basis of the hypothesis that the reduction of glycolaldehyde to ethylene glycol should detoxify glycolaldehyde, we developed a strain overexpressing the alcohol dehydrogenase gene ADH1. The ADH1-overexpressing strain exhibits an improved fermentation profile in a glycolaldehyde-containing medium. The conversion ratio of glycolaldehyde to ethylene glycol is 30 ± 1.9% when the control strain is used; this ratio increases to 77 ± 3.6% in the case of the ADH1-overexpressing strain. A glycolaldehyde treatment and the overexpression of ADH1 cause changes in the fermentation products so as to balance the metabolic carbon flux and the redox status. Finally, the ADH1-overexpressing strain shows a statistically significantly improved fermentation profile in a hot-compressed water-treated cellulose-containing medium. The conversion ratio of glycolaldehyde to ethylene glycol is 33 ± 0.85% when the control strain is used but increases to 72 ± 1.7% in the case of the ADH1-overexpressing strain. These results show that the reduction of glycolaldehyde to ethylene glycol is a promising strategy to decrease the toxicity of hot-compressed water-treated cellulose. This is the first report on the improvement of yeast tolerance to hot-compressed water-treated cellulose and glycolaldehyde.

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Model Studies on Chemical and Textural Modifications in Gelatin Films by Reaction with Glyoxal and Glycolaldehyde

Cited by 21 publications

References 29 publications

Treatments of protein for biopolymer production in view of processability and physical properties: A review

Treatments of protein for biopolymer production in view of processability and physical properties: A review

Glycolaldehyde‐modified β‐lactoglobulin AGEs are unable to stimulate inflammatory signaling pathways in RAGE‐expressing human cell lines

Improvement of tolerance of Saccharomyces cerevisiae to hot-compressed water-treated cellulose by expression of ADH1

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