Abstract: The present disclosure belongs to the technical field of lubricating material preparation, and specifically relates to a halloysite nanotube (HNT)-encapsulated ionic liquid (IL) microcapsule, a self-lubricating fiber textile composite, and a preparation method and use thereof. In the present disclosure, the preparation method includes the following steps: dispersing a HNT and an alkali metal salt of a saturated fatty acid in water, dispersing a resulting inner surface-modified HNT and an IL in an organic solvent, injecting the IL into the HNT in the mixed dispersion under vacuumizing to obtain an IL-filled HNT, and encapsulating a resulting IL-filled HNT at a tube end with an encapsulating material to obtain the HNT-encapsulated IL microcapsule.

Abstract: The present invention relates to the field of genetic engineering, particularly to phytase variant YeAPPA having improved pepsin resistance and acid resistance, and increased catalytic efficiency, by substituting Leucine at the 162th site of the sequence set forth in SEQ ID NO.1 with glycine or proline or substituting glutamic acid at the 230th site of the sequence set forth in SEQ ID NO.1 with glycine, proline or arginine, in the benefit of the development of economical feed enzyme industry.

Abstract: The present invention relates to the field of genetic engineering, particularly to phytase variants YkAPPA having amino acid sequence substituting Leucine at the 162th site of the sequence set forth in SEQ ID NO.1 with glycine or proline, or having amino acid sequence substituting glutamic acid at the 230th site of the sequence set forth in SEQ ID NO.1 with glycine, alanine, serine, threonine, aspartic acid, proline, or arginine, and having improved pepsin resistance and increased catalytic efficiency of 2.1 times of that of the wild phytase, in the benefit of the development of economical feed enzyme industry.

Abstract: Provided are a fungus-sourced high-temperature neutral Family-45 cullulase as well as a coding gene and application thereof. The cullulase has optimal pH value of 5.5, and optimal temperature of 60° C., has certain enzyme activity in alkaline condition, and has good alkali resistance, maintains about 70% enzyme activity in optimal condition after being processed at 90° C. for 1 hour, maintains about 50% enzyme activity in optimal condition after being processed in boiling water for 1 hour, and can be well applied in c and other fields.

Abstract: The present invention relates to the field of genetic engineering, particularly to phytase variants YkAPPA having amino acid sequence substituting Leucine at the 162th site of the sequence set forth in SEQ ID NO.1 with glycine or proline, or having amino acid sequence substituting glutamic acid at the 230th site of the sequence set forth in SEQ ID NO.1 with glycine, alanine, serine, threonine, aspartic acid, proline, or arginine, and having improved pepsin resistance and increased catalytic efficiency of 2.1 times of that of the wild phytase, in the benefit of the development of economical feed enzyme industry.

Abstract: The present invention relates to the field of genetic engineering, particularly to phytase variant YeAPPA having improved pepsin resistance and acid resistance, and increased catalytic efficiency, by substituting Leucine at the 162th site of the sequence set forth in SEQ ID NO.1 with glycine or proline or substituting glutamic acid at the 230th site of the sequence set forth in SEQ ID NO.1 with glycine, proline or arginine, in the benefit of the development of economical feed enzyme industry.

Abstract: Provided are a fungus-sourced high-temperature neutral Family-45 cullulase as well as a coding gene and application thereof. The cullulase has optimal pH value of 5.5, and optimal temperature of 60° C., has certain enzyme activity in alkaline condition, and has good alkali resistance, maintains about 70% enzyme activity in optimal condition after being processed at 90° C. for 1 hour, maintains about 50% enzyme activity in optimal condition after being processed in boiling water for 1 hour, and can be well applied in c and other fields.

Abstract: Provided are a fungus-sourced high-temperature acid ?-glucosidase as well as a coding gene, and an application thereof. The provide ?-glucosidase has the optimal pH value of 4.5 and the optimal temperature of 75° C., and maintains over 90% enzyme activity in the optimal condition after being processed at 60° C. for 1 h. The re-engineering yeast strain GS115/bgl3A of the coding gene comprising the ?-glucosidase has high fermentation level.

Abstract: Provided are a fungus-sourced high-temperature acid ?-glucosidase as well as a coding gene, and an application thereof. The provide ?-glucosidase has the optimal pH value of 4.5 and the optimal temperature of 75° C., and maintains over 90% enzyme activity in the optimal condition after being processed at 60° C. for 1 h. The re-engineering yeast strain GS115/bgl3A of the coding gene comprising the ?-glucosidase has high fermentation level.

Abstract: The present invention relates to the field of genetic engineering, in particular, the present invention relates to a method for producing a phytase variant with an improved thermal stability, and a phytase variant and the use thereof. The phytase variant contains at least one proline modification, compared to the phytase from Escherichia coli and other mutants thereof. The phytase variants with the modification have preferably improved properties, such as the thermal stability, optimal reaction temperature, pH property, specific activity, protease resistance and performance in animal feeds.

Abstract: The present invention relates to the field of genetic engineering, in particular, the present invention relates to a method for producing a phytase variant with an improved thermal stability, and a phytase variant and the use thereof. The phytase variant contains at least one proline modification, compared to the phytase from Escherichia coli and other mutants thereof. The phytase variants with the modification have preferably improved properties, such as the thermal stability, optimal reaction temperature, pH property, specific activity, protease resistance and performance in animal feeds.

Abstract: The present invention relates to a novel phytase enzyme, a novel isolated nucleic acid molecule coding the enzyme, and a novel Yersinia intermedia having phytase activity. Particularly, the present invention relates to the phytase having (a) Theoretical molecular weight 45.5 kDa, (b) high specific activity 3960±248 U/mg, (c) high stability at high temperature and wide pH, (d) optimal pH of 4.0-5.0, (e) optimal temperature of 50-60° C., (f) high resistance to pepsin and trypsin. The phytase is very suitable to be used in feed of monogastrics as feed additive. The present invention also relates to a recombinant vector comprising said nucleic acid molecule, a recombinant host cell (e.g., Pichia pastoris) harboring said recombinant vector, and a method for producing phytase using the recombinant host cell. The present invention further provides a feed additive comprising said phytase and/or host cells expressing a phytase as effective ingredient.

Abstract: The present invention relates to a novel phytase enzyme, a novel isolated nucleic acid molecule coding the enzyme, and a novel Yersinia intermedia having phytase activity. Particularly, the present invention relates to the phytase having (a) Theoretical molecular weight 45.5 kDa, (b) high specific activity 3960±248 U/mg, (c) high stability at high temperature and wide pH, (d) optimal pH of 4.0-5.0, (e) optimal temperature of 50-60° C., (f) high resistance to pepsin and trypsin. The phytase is very suitable to be used in feed of monogastrics as feed additive. The present invention also relates to a recombinant vector comprising said nucleic acid molecule, a recombinant host cell (e.g., Pichia pastoris) harboring said recombinant vector, and a method for producing phytase using the recombinant host cell. The present invention further provides a feed additive comprising said phytase and/or host cells expressing a phytase as effective ingredient.