Magnetic Janus SiO nanoparticles immobilized protease mutant T70I as a novel clarification agent for juice processing.

The juice processing industry offers several benefits, including promoting health and wellness through the delivery of beverages rich in nutrients. Nonetheless, the industry encounters significant challenges regarding new technologies for processing and preservation given that they can be costly and labor-intensive. In this study, magnetic Janus silica (SiO) nanoparticle which offers multifunctionality and high stability was synthesized and subsequently immobilized with a protease mutant T70I (T70I@MSNs) to serve as a clarifying agent in juice.

Mulberry (Morus alba L.) leaf powder modified the processing of meat alternatives: Principal component analysis from apparent properties to chemical bonds.

For texture control in plant-meat alternatives, the interrelationship between apparent characteristics and chemical bonds in high-fiber formulations remains unclear. The influence of mulberry leaf powder on apparent characteristics and chemical bonds of raw materials, block and strip products at addition amounts of 0.5-25% was analyzed.

Silkworm pupae protein co-degradation by magnetic nanoparticles immobilized proteinase K and Mucor circinelloides aspartic protease for further utilization of sericulture by-products.

Silkworm pupae, by-product of sericulture industry, is massively discarded. The degradation rate of silkworm pupae protein is critical to further employment, which reduces the impact of waste on the environment. Herein, magnetic Janus mesoporous silica nanoparticles immobilized proteinase K mutant T206M and Mucor circinelloides aspartic protease were employed in the co-degradation.

Molecular modification and biotechnological applications of microbial aspartic proteases.

The growing preference for incorporating microbial aspartic proteases in industries is due to their high catalytic function and high degree of substrate selectivity. These properties, however, are attributable to molecular alterations in their structure and a variety of other characteristics. Molecular tools, functional genomics, and genome editing technologies coupled with other biotechnological approaches have aided in improving the potential of industrially important microbial proteases by addressing some of their major limitations, such as: low catalytic efficiency, low conversion rates, low thermostability, and less enzyme yield.

Advances in the One-Step Approach of Polymeric Materials Using Enzymatic Techniques.

The formulation in which biochemical enzymes are administered in polymer science plays a key role in retaining their catalytic activity. The one-step synthesis of polymers with highly sequence-controlled enzymes is a strategy employed to provide enzymes with higher catalytic activity and thermostability in material sustainability. Enzyme-catalyzed chain growth polymerization reactions using activated monomers, protein-polymer complexation techniques, covalent and non-covalent interaction, and electrostatic interactions can provide means to develop formulations that maintain the stability of the enzyme during complex material processes.

More efficient barley malting under catalyst: Thermostability improvement of a β-1,3-1,4-glucanase through surface charge engineering with higher activity.

β-1,3-1,4-Glucanase is an indispensable biocatalyst in barley brewing industry for its crucial effect in reducing the viscosity of mash. However, the unsatisfactory thermostability greatly limited its application performance. In this study, structure-based surface charge engineering was conducted aiming at thermostability improvement of BisGlu16B, a highly active β-1,3-1,4-glucanase from Bispora sp.

Long noncoding RNA transcriptome analysis reveals novel lncRNAs in Morus alba 'Yu-711' response to drought stress.

Drought stress has been a key environmental factor affecting plant growth and development. The plant genome is capable of producing long noncoding RNAs (lncRNAs). To better understand white mulberry (Morus alba L.

Loop engineering of a thermostable GH10 xylanase to improve low-temperature catalytic performance for better synergistic biomass-degrading abilities.

Lignocellulosic biorefining for producing biofuels poses technical challenges. It is usually conducted over a long time using heat, making it energy intensive. In this study, we lowered the energy consumption of this process through an optimized enzyme and pretreatment strategy.

Dual promoter strategy enhances co-expression of α-L-rhamnosidase and enhanced fluorescent protein for whole-cell catalysis and bioresource valorization.

Developing circular economy is the only way to improve the efficiency of resource utilization. Whole-cell catalysis is an effective method to recycle enzymes, improve catalytic efficiency, and reduce production costs. The enzyme, α-L-rhamnosidase has considerable application prospects in the field of biocatalysis as it can hydrolyze a variety of α-L rhamnoses.

Improvement in catalytic activity and thermostability of a GH10 xylanase and its synergistic degradation of biomass with cellulase.

Background: Xylanase is one of the most extensively used biocatalysts for biomass degradation. However, its low catalytic efficiency and poor thermostability limit its applications. Therefore, improving the properties of xylanases to enable synergistic degradation of lignocellulosic biomass with cellulase is of considerable significance in the field of bioenergy.

Microfluidic tools for lipid production and modification: a review.

Microfluidics has great potential as an efficient tool for a large range of applications in industry. The ability of such devices to deal with an extremely small amount of fluid has additional benefits, including superlatively fast and efficient mass and heat transfer. These characteristics of microfluidics have attracted an enormous amount of interest in their use as a novel tool for lipid production and modification.