Improving gelling properties of myofibrillar proteins incorporating with cellulose micro/nanofibres

The effects of cellulose microfibres (CMFs, Average size: 100 ± 5 μm) and cellulose nanofibres (CNFs, Average size: 60 ± 3 nm) on the properties of myofibrillar protein (MP) gels from duck breast meat were studied. The results demonstrated that CMFs and CNFs were mostly connected to MP by non-covalent bonds, the diffusion and cross-linking of MP molecules was promoted, and a denser and more complete gel network was formed. With the increases of CMFs and CNFs concentration (0–10%), the hardness was increased by 13.15% and 19.78% for CMFs10% and CNFs10% gels, respectively, and the elasticity was increased by 40% and 80%, respectively. At the same concentration (0–10%), the increase in gel hardness, viscoelasticity and immobilised water content was greater in the CNFs-MP group than in the CMFs-MP group. The CNFs-MP group had a tighter gel network, and CNFs had a better potential to improve the gelation performance of MP.     

The effect of rice bran on physicochemical,textural and glycaemic properties of ready-to-eat extruded corn snacks

In this work, corn extruded snack products were enriched with rice bran (RB) at 10% and 15%. A co-rotating twin-screw extruder was used with a feed moisture content of 16 g 100 g⁻¹, a screw speed of 240 r.p.m. and four heating sections of the barrel (100, 140, 150 and 150 °C). The impact of RB inclusion on nutritional profile, starch digestion, physicochemical and textural properties of snack products was evaluated. RB-enriched extrudates showed a lower specific volume and hardness and higher crispness than control. RB at 15% gave a water-holding capacity lower than control. Rheology of extrudate dispersions indicated an increase in elastic interactions and solid-like behaviour with RB supplementation. Differences in rheological properties resulted in attenuation of predictive glycaemic response for RB-enriched snacks.     

Effect of microwave heating time on the gel properties of chicken myofibrillar proteins and their formation mechanism

The present work was conducted to illustrate the mechanism of gel formation of myofibrillar proteins (MPs) under different microwave heating times. The results showed that the denaturation enthalpy (ΔH) of the MPs significantly decreased when the heating time increased from 3 to 9 s and then completely disappeared as the heating time progressed, indicating that the MPs gradually denatured and subsequently aggregated with increasing heating time, which was further verified by the changes in the secondary structure, electrophoretic bands, and gel properties (e.g., water holding capacity and textural profiles) of the MPs. Microstructural images indicated that the MP gel formed under 12 s had the most compact network, indicating that extended microwave heating time could induce quality deterioration of MP gels. Moreover, the hydrophobic forces, electrostatic forces, and disulphide bonds of the MPs gradually intensified with increasing microwave heating time, suggesting that both non-covalent and covalent bonds could promote molecular denaturation and subsequent aggregation of MPs. In addition, correlation analysis revealed that the changes in the molecular conformation of MPs induced by different microwave heating times could effectively regulate the formation of MP gels and their related properties.     

Characterization of a Tryptophan 6-Halogenase from Streptomyces albus and Its Regioselectivity Determinants

Tryptophan halogenases are found in diverse organisms and catalyze regiospecific halogenation. They play an important role in the biosynthesis of halogenated indole alkaloids, which are biologically active and of therapeutic importance. Here, a tryptophan 6-halogenase (SatH) from Streptomyces albus was characterized by using a whole-cell reaction system in Escherichia coli. SatH showed substrate specificity for chloride and bromide ions, leading to regiospecific halogenation at the C6-position of l -tryptophan. In addition, SatH exhibited higher performance in bromination than that of previously reported tryptophan halogenases in the whole-cell reaction system. Through structure-based protein mutagenesis, it has been revealed that two consecutive residues, A78/V79 in SatH and G77/I78 in PyrH, are key determinants in the regioselectivity difference between tryptophan 6- and 5-halogenases. Substituting the AV with GI residues switched the regioselectivity of SatH by moving the orientation of tryptophan. These data contribute to an understanding of the key residues that determine the regioselectivity of tryptophan halogenases.     

Combined effects of wheat gluten and carboxymethylcellulose on dough rheological behaviours and gluten network of potato–wheat flour-based bread

Incorporating high level of potato flour into wheat flour enhances nutritional values of bread but induces a series of problems that lead to the decline of the bread quality. To overcome the barrier, wheat gluten and carboxymethylcellulose (CMC) were added into potato–wheat composite flour to improve dough machinability and bread quality. The rheological properties, thermo-mechanical properties and microstructures of dough were investigated. The results showed that the interaction between gluten and CMC mitigated the discontinuity of gluten matrix and gluten protein aggregation caused by the addition of potato flour, which yielded a more branched and compact gluten network. The compact three-dimensional viscoelastic structure induced improvements of gas retention capacity and dough stability, making it mimic the machinability properties of wheat flour dough. Bread qualities were apparently improved with the combined use of 4% gluten and 6% CMC, of which specific volume increased by 42.86%, and simultaneously, hardness reduced by 75.93%.     

Design,Synthesis, and Self-Assembly Studies of a Suite of Monodisperse,Facially Amphiphilic,Protein–Dendron Conjugates

The custom design of protein–dendron amphiphilic macromolecules is at the forefront of macromolecular engineering. Macromolecules with this architecture are very interesting because of their ability to self-assemble into various biomimetic nanoscopic structures. However, to date, there are no reports on this concept due to technical challenges associated with the chemical synthesis. Towards that end, herein, a new chemical methodology for the modular synthesis of a suite of monodisperse, facially amphiphilic, protein–dendron bioconjugates is reported. Benzyl ether dendrons of different generations (G1–G4) are coupled to monodisperse cetyl ethylene glycol to form macromolecular amphiphilic activity-based probes (AABPs) with a single protein reactive functionality. Micelle-assisted protein labeling technology is utilized for site-specific conjugation of macromolecular AABPs to globular proteins to make monodisperse, facially amphiphilic, protein–dendron bioconjugates. These biohybrid conjugates have the ability to self-assemble into supramolecular protein nanoassemblies. Self-assembly is primarily mediated by strong hydrophobic interactions of the benzyl ether dendron domain. The size, surface charge, and oligomeric state of protein nanoassemblies could be systematically tuned by choosing an appropriate dendron or protein of interest. This chemical method discloses a new way to custom-make monodisperse, facially amphiphilic, protein–dendron bioconjugates.     

Site-Specific PEGylation of Therapeutic Proteins

The use of proteins as therapeutics has a long history and is becoming ever more common in modern medicine. While the number of protein-based drugs is growing every year, significant problems still remain with their use. Among these problems are rapid degradation and excretion from patients, thus requiring frequent dosing, which in turn increases the chances for an immunological response as well as increasing the cost of therapy. One of the main strategies to alleviate these problems is to link a polyethylene glycol (PEG) group to the protein of interest. This process, called PEGylation, has grown dramatically in recent years resulting in several approved drugs. Installing a single PEG chain at a defined site in a protein is challenging. Recently, there is has been considerable research into various methods for the site-specific PEGylation of proteins. This review seeks to summarize that work and provide background and context for how site-specific PEGylation is performed. After introducing the topic of site-specific PEGylation, recent developments using chemical methods are described. That is followed by a more extensive discussion of bioorthogonal reactions and enzymatic labeling.