A hierarchical catalyst composition comprising a continuous or particulate macroporous scaffold in which is incorporated mesoporous aggregates of magnetic nanoparticles, wherein an enzyme is embedded in mesopores of the mesoporous aggregates of magnetic nanoparticles. Methods for synthesizing the hierarchical catalyst composition are also described. Also described are processes that use the recoverable hierarchical catalyst composition for depolymerizing lignin, remediation of water contaminated with aromatic substances, polymerizing monomers by a free-radical mechanism, epoxidation of alkenes, halogenation of phenols, inhibiting growth and function of microorganisms in a solution, and carbon dioxide conversion to methanol. Further described are methods for increasing the space time yield and/or total turnover number of a liquid-phase chemical reaction that includes magnetic particles to facilitate the chemical reaction, the method comprising subjecting the chemical reaction to a plurality of magnetic fields of selected magnetic strength, relative position in the chemical reaction, and relative motion.

A peroxidase, a method for producing the peroxidase, and an agent including at least one peroxidase are provided herein. The peroxidase includes an amino acid sequence that has a sequence identity of at least 60% to the amino acid sequence specified in SEQ ID NO:1 (Gap MnP1), across the entire length thereof; or has a sequence identity of at least 60% to the amino acid sequence specified in SEQ ID NO:2 (Gap MnP2), across the entire length thereof; or has a sequence identity of at least 80% to the amino acid sequence specified in SEQ ID NO:3 (Bja LiP), across the entire length thereof; or has a sequence identity of at least 60% to the amino acid sequence specified in SEQ ID NO:4 (Bja DyP), across the entire length thereof.

The technical field of enzyme immobilization, and particularly, an organic-inorganic hybrid nanoflower and a preparation method thereof. The organic-inorganic hybrid nanoflower is a flower-like immobilized enzyme formed by self-assembly of a layered rare earth compound as an inorganic carrier and a biological enzyme as an organic component. The layered rare earth compound is Ln.sub.2(OH).sub.5NO.sub.3.nH.sub.2O, where Ln is one or more of La, Ce, Pr, Nd, Sm, Eu, Gd, Tb, Dy, Ho, Er, Tm, Yb, or Y, and n=1.1-2.5. The biological enzyme is one or more of α-amylase, horseradish peroxidase, or laccase. A layered rare earth compound is used as the inorganic carrier for the organic biological enzyme to form the flower-like immobilized enzyme. The immobilized enzyme has better stability and higher catalytic performance when compared with a free enzyme.

The present invention relates to a method for expressing, water-solubilizing, and purifying protein by using a calsequestrin-tag (CSQ-tag). Provided are: a recombinant expression vector containing a CSQ-tag and a target protein; a host cell transformed using the recombinant expression vector; and a method for expressing and purifying a target protein by using a CSQ tag. The present invention uses CSQ-tags to increase the expression of proteins that are widely used in pharmaceuticals and cosmetics, and allows the proteins to be easily separated by calcium, and thus is expected to be able to lower the cost of protein materials and protein pharmaceuticals.

The invention relates to a recombinant Marasmius rotula unspecific peroxygenase (rMroURO) and two mutants thereof, wherein said mutants show enhanced selectivity towards either the epoxidation or the (sub)terminal ω/(ω-1)-hydroxylation of unsaturated fatty acids. The invention also refers to the use of these enzyme variants for the specific epoxidation or hydroxylation of fatty acids such as oleic acid, linoleic acid and/or alpha-linolenic acid.

The present invention relates to transgenic microalgae for the production of cell wall degradative enzymes having a heat-stable cellulolytic activity (HCWDEs) and their relative uses in the biodegradation of cellulose or lignocellulose sources in the industrial field.

A method for manufacturing a fraction comprising the proteins lactoferrin and/or lactoperoxidase from a source containing at least one of these proteins wherein the source is selected from the group consisting of milk, colostrum, acid or sweet whey, by means of a chromatographic separation process with a monolithic column having cation exchanger properties, wherein in the separation process a pH gradient or a combined pH and salt gradient elution is employed after loading the source to the column.

Further disclosed is a composition of matter comprising lactoferrin having a C value of >60% and A value of >1% or lactoperoxidase.

Compositions and methods for anti-oxidant therapy are provided.

The embodiments disclosed herein utilized RNA targeting effectors to provide a robust CRISPR-based diagnostic with attomolar sensitivity. Embodiments disclosed herein can detect both DNA and RNA with comparable levels of sensitivity and can differentiate targets from non-targets based on single base pair differences, and includes detection by colorimetric and/or fluorescence shifts. Moreover, the embodiments disclosed herein can be prepared in freeze-dried format for convenient distribution and point-of-care (POC) applications. Such embodiments are useful in multiple scenarios in human health including, for example, viral detection, bacterial strain typing, sensitive genotyping, and detection of disease-associated cell free DNA.

A process for site-specific immobilization of an enzyme on a polymer involving pairing of an enzyme and polymer to optimize cross-linking between the enzyme and the polymer while avoiding conformational or biochemical inhibition of enzyme activity. The process involves site specific interaction in a multiple phase synthesis within a buffered reaction medium and in an inert atmosphere. The reaction kinetics of the conjugation are modulated by chilling the reaction medium containing the enzyme and polymer to about the maximum solvent density of the reaction medium. The cross-linking of the enzyme and a polymer pair performed produces an enzymatically active, stable conjugate.