The plastics sunset and the bioplastics sunrise

Plastics has been an integral part of our lives for the last century as the main material for various useful commodity items. Irony of fate, the same specific properties that make plastics ideal to create such a wide range of products are also responsible for the present dramatic environmental pollution. What suggestions do the technological innovations currently suggest to solve this worldwide problem? Among the others, one is to replace the traditional plastics with alternative materials derived from non-oil polymers capable of being degraded in months and not in years or centuries. But the research in this field is relatively new and undoubtedly there are still developments that need to be made. Thus, we must be aware that the plastic age is at sunset and the bio-plastics sun is just rising on the horizon

Protein Crosslinks Influence Food Digestion

Enzymatic crosslinking is increasingly applied to confer specific properties to different proteins and, consequently, to food products of which they are components. Among the most investigated enzymes, transglutaminases (in particular the microbial isoform, mTG) and various oxidative biocatalysts are having special attention by food biotechnology researchers. mTG catalyzes isopeptide bond formation among protein molecules, leading to inter-molecular crosslinks and being able to produce both homo- and hetero-polymers. Its peculiar properties, such as the calcium independency, the broad substrate specificity, the stability over a wide range of temperatures and pH values, make such enzyme an effective tool to modify the characteristics of many protein-based foods

Protein Crosslinks Influence Food Digestion

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Functional properties of rye prolamin (secalin) and their improvement by protein lipophilization through capric acid covalent binding

Secalin (SCL), the prolamin fraction of rye protein, was chemically lipophilized using acylation reaction by treatment with different amounts of capric acid chloride (0, 2, 4, and 6 mmol/g) to enhance its functional properties. It was shown that SCL lipophilization increased the surface hydrophobicity and the hydrophobic interactions, leading to a reduction in protein solubility and water absorption capacity and to a greater oil absorption. In addition, SCL both emulsifying capacity and stability were improved when the protein was treated with low amount of capric acid chloride. Finally, the foaming capacity of SCL markedly increased after its treatment with increasing concentrations of the acylating agent, even though the foam of the modified protein was found to be more stable at the lower level of protein acylation. Technological application of lipophilized SCL as a protein additive in food preparations is suggested

Tuning the functional properties of bitter vetch (Vicia ervilia) protein films grafted with spermidine

Bitter vetch protein films containing positively charged spermidine, alone or with low amounts of glycerol, showed high tensile strength that progressively decreased by increasing the plasticizer concentration. Accordingly, lower film elongation at break and higher Young’s module values were detected in the presence of the polyamine without or with small amounts of glycerol. These data suggest that spermidine not only acts as a plasticizer itself by ionically interacting with proteins, but that it also facilitates glycerol-dependent reduction of the intermolecular forces along the protein chains, consequently improving the film flexibility and extensibility. Thus, spermidine may be considered not only as a primary, but also as a secondary plasticizer because of its ability to enhance glycerol plasticizing performance. Such double behavior of the polyamine was confirmed by the film permeability tests, since spermidine increased the barrier properties to gases and water vapor, while glycerol emphasized this effect at low concentrations but led to its marked reversal at high concentrations. Film microscopic images also substantiated these findings, showing more compact, cohesive, and homogeneous matrices in all spermidine-containing films. © 2017 by the authors. Licensee MDPI, Basel, Switzerland

Biosynthesis of Polyamines in Mouse Brain: Effects of Methionine Sulfoximine and Adenosylhomocysteine

This study examines the consequences on cerebral polyamine biosynthesis of increases and decreases in cerebral methylation. Increases were elicited by administering the convulsant agent methionine sulfoximine (MSO) and decreases by elevating in vivo the cerebral levels of the methylation inhibitor S -adenosyl-homocysteine. Following the intraventricular (i.vt.) administration of one of the two possible polyamine precursors, [1,4- 14 C]putrescine, the specific radioactivity (sra) of the newly formed [ 14 C]spermidine remained unchanged. Conversely, after i.vt. l-[3,4- 14 C]methionine, the other polyamine precursor, significantly higher sra values for [ 14 C]spermidine and [ 14 C]spermine were recorded in the brains of the MSO-treated animals. [ 14 C] S - adenosylmethionine in the brain of the MSO-treated animals was also more highly labeled following [1- 14 C]-methionine, indicating its accelerated formation relative to controls. We also investigated the effect of the administration of adenosine + homocysteine, a treatment that results in elevated brain adenosylhomocysteine levels, on polyamine biosynthesis from [3,4- 14 C]-methionine. The results of these experiments show both significantly lower sra values for [ 14 C]spermidine and [ 14 C]spermine and significantly higher than control endogenous methionine levels, a clear sign of the existence of a retardation in the conversion of methionine to polyamines under these conditions. In conclusion, the present study demonstrates that while interference with cerebral methylation results in significant alterations of the rate of formation of the methionine moiety of spermidine and spermine, it has no effect on the entry of the putrescine moiety into the two polyamine molecules.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/66159/1/j.1471-4159.1983.tb08055.x.pd

Transglutaminase-catalyzed preparation of chitosan-ovalbumin films

Microbial transglutaminase was employed as catalyst for preparing chitosan–ovalbumin films. The films showed low solubility at a wide range of pH and underwent to a good enzymatic hydrolysis with trypsin. The degree of swelling was reduced and the mechanical resistance of the chitosan–ovalbumin films increased from 24 to 35MPa after enzymatic treatment with transglutaminase. The barrier efficiency toward water vapour was slightly improved for the films prepared by transglutaminase-mediated cross-linking

Swelling, mechanical and barrier properties of albedo-based films prepared in the presence of phaseolin crosslinked or not by transglutaminase

Edible films were obtained from Citrus paradisi grapefruit albedo homogenates and bean protein phaseolin modified or not by the enzyme transglutaminase. Swelling capability, barrier performance to water vapor, oxygen and carbon dioxide, and mechanical properties of such films were investigated. The addition of the protein, mostly in the presence of transglutaminase, provide films less swellable at pH values above 5 compared to films made by albedo homogenates only, whereas the action of the enzyme clearly improves mechanical properties producing more stretchable and elastic films. Moreover, transglutaminase-mediated cross-linking of phaseolin gives rise to films less permeable to carbon dioxide and able to offer a high barrier to water vapor. These findings suggest that albedo-phaseolin film prepared in the presence of transglutaminase can be a promising candidate to be used as food edible wrap

Rapid assay of spermidine synthase activity by high-performance liquid chromatography

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/24196/1/0000455.pd