Publications by authors named "Luyao Bian"

The development and manufacture of high-quality starch are a new research focus in food science. Here, transglutaminase was used in the wet processing of glutinous rice flour to prepare customized sweet dumplings. Transglutaminase (0.

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The escalating threat of malachite green (MG) pollution poses significant risks to ecosystems. Saturation mutation targeting Tyr230 of small laccase (SLAC) from Streptomyces coelicolor yielded Y230R, exhibiting a remarkable 104 % increase in specific activity. Notably, this mutation achieved dual enhancements in both activity and pH stability.

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Glutinous rice is extensively consumed due to its nutritious content and wonderful flavor. However, glutinous rice flour has a high glycemic index, and the storage deterioration of sweet dumplingsissevere. Transglutaminase (TG) was used to cross-link glutinous rice protein and improve the characteristics of glutinous rice products.

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Malachite green (MG) poses a formidable threat to ecosystems and human health. Laccase emerges as a promising candidate for MG degradation, prompting an investigation into the catalytic activity modulation of a small laccase (SLAC) from , with a focus on amino acid position 228. Through saturation mutagenesis, five mutants with a 50% increase in the specific activity were generated.

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This investigation examined how the laccase (rBVL-MRL522) influenced the physicochemical characteristics, structural attributes, and functional capabilities of both dough and noodles. Incorporating rBVL-MRL522 (1 U/g) did not lead to a substantial change in the water absorption of wheat flour. However, the introduction of rBVL-MRL522 caused a significant elongation in the formation time of wheat flour dough, extending it by 88.

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In response to the growing demand for biodegraded film with high mechanical properties for complex preservation application scenarios, we developed a curdlan (CD) blended films with exceptional mechanical strength through an alkali dissolution method. Notably, the alkali-soluble CD film exhibited five-fold increase in tensile strength (TS) when compared to its water-soluble counterpart. Furthermore, the inclusion of 2 % bacterial cellulose (BC) resulted in a significant 41.

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Bio-enzymatic grafting phenolic acid to chitosan derivative is an efficient and environmentally friendly molecular synthesis technology. In the present study, N-carboxymethyl chitosan (CMCS) was grafted with gallic acid (GA) using recombinant bacterial laccase from as a catalyst. GA and CMCS were successfully grafted as determined by measuring amino acid content, Fourier transform infrared (FTIR) spectroscopy and ultraviolet-visible (UV-Vis) spectroscopy.

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Bioenzymatic degradation of aflatoxin B1 (AFB1) is a safe, efficient and environmentally friendly detoxification technology. In this work, AFB1 was successfully degraded by recombinant laccase (fmb-rL103) in the absence of a mediator. The laccase gene was cloned from Bacillus vallismortis fmb-103, and was expressed in heterologous host Escherichia coli after codon optimization.

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With the increasing attention to food preservation and environmental safety, there is great pressing demand to explore novel edible and environment-friendly food packaging films. In the present study, a new kind natural curdlan (CD) film was developed with the addition of bacterial cellulose (BC) and cinnamon essential oil (CEO) at 2% and 10% (w/w) amounts, with regard to improve mechanical properties and investigate potential food applications. Our results showed that the tensile strength, the crystallinity and the thermal stability of the CD/BC blending film were improved, while the water vapor permeability, moisture content and the lightness were reduced.

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In this study, to improve the mechanical and thermal properties of curdlan film, a curdlan/nanocellulose (NC) blended film was prepared and characterized for the first time. NC was successfully prepared from microcrystalline cellulose (MCC) with NaOH/urea treatment. The particle size of NC was observed to be 70-140 nm by cryo-electron microscope (cryo-EM).

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