A hydrogel-based biological delivery vehicle used to effectively deliver drug and biological material to tissue or organ sites. More specifically, a hydrogel binding matrix having a biopolymer backbone containing carboxyl groups. Tyramine may be substituted for at least a portion of the carboxyl groups, so that, when hydrogen peroxide is added, it causes creation of covalent bonds between tyramine molecules and cross-links the hydrogel binding matrix, thereby enabling the hydrogel binding matrix to transition from liquid to gel state. The hydrogel binding matrix, in its liquid form, is capable of encapsulating drug reservoirs to create a homogenous liquid with evenly distributed particles containing drugs or target molecules. As the hydrogel binding matrix solidifies into a gel state, the newly created cross-links do not disrupt or react with the drugs or target molecules contained within the drug reservoirs. This hydrogel-based biological delivery vehicle can be used in several medical applications.

Methods of treating a tumor in a subject include identifying a subject having, at risk for, or suspected of having a tumor, and administering to the subject an effective amount of an SRPX.

The present invention discloses an engineering yeast strain for producing nervonic acids. The yeast strain over-expresses the genes related to enzymes required in a synthetic process of long-chain unsaturated fatty acids, such as fatty acid elongase, desaturase, diacylglycerol acyltransferase and the like, and optionally, further adjusts and controls the synthesis and decomposition route of triglyceride, the synthesis and decomposition route of sphingomyelin, and the synthesis and decomposition route and the oxidation-reduction balanced route of lipid subcell levels. The recombinant yeast strain can produce microorganism oil; and the content of the prepared nervonic acids accounts for 39.6% of the total fatty acids.

The present invention is a multivalent immunogenic composition for immunizing an animal against filariasis. In some embodiments, the antigens of the multivalent immunogenic composition are protein-based, DNA-based, or a combination thereof. This invention also provides a method and kit for detecting a filarial nematode and determining vaccine efficacy.

A hydrogel-based biological delivery vehicle used to effectively deliver drug and biological material to tissue or organ sites. More specifically, a hydrogel binding matrix having a biopolymer backbone containing carboxyl groups. Tyramine may be substituted for at least a portion of the carboxyl groups, so that, when hydrogen peroxide is added, it causes creation of covalent bonds between tyramine molecules and cross-links the hydrogel binding matrix, thereby enabling the hydrogel binding matrix to transition from liquid to gel state. The hydrogel binding matrix, in its liquid form, is capable of encapsulating drug reservoirs to create a homogenous liquid with evenly distributed particles containing drugs or target molecules. As the hydrogel binding matrix solidifies into a gel state, the newly created cross-links do not disrupt or react with the drugs or target molecules contained within the drug reservoirs. This hydrogel-based biological delivery vehicle can be used in several medical applications.

The present invention provides use of a manganese peroxidase in the detoxification of mycotoxins, and specifically, the present invention provides five manganese peroxidases (MnP-1, MnP-2, MnP-4, MnP-5, and MnP-6), genes thereof, and uses thereof. The present invention provides five manganese peroxidases (MnP-1, MnP-2, MnP-4, MnP-5, and MnP-6) derived from lignocellulose degradation bacteria, the amino acid sequences thereof being as set forth in SEQ ID NO: 1, SEQ ID NO: 4, SEQ ID NO: 7, SEQ ID NO: 10, and SEQ ID NO: 13.

The present invention provides methods for producing a heme peroxidase from inclusion bodies (IBs) comprising the steps of: providing the heme peroxidase in the form of IBs, solubilizing said IBs, transferring said solubilized IBs into a refolding buffer to obtain a refolding mix, adding a heme cofactor to said refolding mix, wherein the addition of the heme cofactor to the refolding mix is distributed over a time period of at least 1 hour. The invention further provides methods for producing heme peroxidase products.

A chemoenzymatic process for the preparation of an oxidized glucose product comprising contacting D-glucose with an enzyme selected from the group consisting essentially of galactose oxidase (GAO), glucose oxidase (GOX), polysaccharide monooxygenase, catalase, animal peroxidase, periplasmic aldehyde oxidase (Pao), unspecific peroxygenase (UPO), lactoperoxidase (LPO), myeloperoxidase (MPO), eosinophil peroxidase (EPO), thyroid peroxidase (TPO), ovoperoxidase, salivary peroxidase, vanadium haloperoxidase, non-mammalian vertebrate peroxidase (POX), peroxidasin (Pxd), bacterial peroxicin (Pxc), invertebrate peroxinectin (Pxt), short peroxidockerin (PxDo), alpha-dioxygenase (aDox), dual oxidase (DuOx), prostaglandin H synthase (PGHS), cyclooxygenase (CyOx), linoleate diol synthase (LDS), variants thereof, and combinations thereof under conditions suitable for the formation of an oxidized intermediate; and contacting the oxidized intermediate with a metal catalyst to form an oxidized glucose product.

Compositions comprising (i) lactate oxidase (LOX) and Catalase (CAT), preferably in a 1:1 molar ratio; or (ii) a fusion polypeptide comprising both LOX and CAT, e.g., LOXCAT, and methods of use thereof for reducing blood lactate levels, increasing blood pyruvate levels, and/or decreasing blood lactate/pyruvate ratio in a subject.

The present invention discloses a method for preparing L-glufosinate ammonium by biological enzymatic de-racemization, a glufosinate ammonium dehydrogenase mutant and a use thereof. The method for preparing L-glufosinate ammonium by biological enzymatic de-racemization includes catalyzing D,L-glufosinate ammonium as a raw material by a multi-enzyme catalysis system to obtain L-glufosinate ammonium. The enzyme catalysis system includes D-amino acid oxidase for catalyzing D-glufosinate ammonium in the D,L-glufosinate ammonium to 2-carbonyl-4-[hydroxy(methyl)phosphonyl]butanoic acid, and a glufosinate ammonium dehydrogenase mutant for catalytically reducing 2-carbonyl-4-[hydroxy(methyl)phosphonyl]butanoic acid to L-glufosinate ammonium. The glufosinate ammonium dehydrogenase mutant is obtained by mutation of glufosinate-ammonium dehydrogenase in wild fungi Thiopseudomonas denitrificans at a mutation site of V377S. The glufosinate ammonium dehydrogenase mutant in the present invention has better catalytic efficiency. When racemic D, L-glufosinate ammonium is used as a substrate for a catalytic reaction, the conversion rate is much higher than the conversion rate of a wild-type enzyme, and the yield of 2-carbonyl-4-[hydroxy(methyl)phosphonyl]butanoic acid (PPO for short) is also greatly improved.