A method for pretreating a wood dust includes conducting a structurally damaged step and an alkali treatment step. In the structurally damaged step, the wood dust is disposed in a scCO.sub.2 atmosphere with a pressure of 2600 psi to 3400 psi at a temperature of 40° C. to 120° C. for a predetermined time, and then the pressure is adjusted to drop to an atmospheric pressure in a sudden manner to obtain a structurally damaged wood dust. In the alkali treatment step, the structurally damaged wood dust is immersed in an alkaline H.sub.2O.sub.2 solution at a temperature of 50° C. to 70° C., a concentration of H.sub.2O.sub.2 in the alkaline hydrogen peroxide solution is in a range of 0.1 wt % to 2.1 wt %, and a pH value of the alkaline H.sub.2O.sub.2 solution is in a range of 10.5 to 12. Thus a treated wood dust is obtained.

A method for pretreating a wood dust includes conducting a structurally damaged step and an alkali treatment step. In the structurally damaged step, the wood dust is disposed in a scCO.sub.2 atmosphere with a pressure of 2600 psi to 3400 psi at a temperature of 40° C. to 120° C. for a predetermined time, and then the pressure is adjusted to drop to an atmospheric pressure in a sudden manner to obtain a structurally damaged wood dust. In the alkali treatment step, the structurally damaged wood dust is immersed in an alkaline H.sub.2O.sub.2 solution at a temperature of 50° C. to 70° C., a concentration of H.sub.2O.sub.2 in the alkaline hydrogen peroxide solution is in a range of 0.1 wt % to 2.1 wt %, and a pH value of the alkaline H.sub.2O.sub.2 solution is in a range of 10.5 to 12. Thus a treated wood dust is obtained.

Methods of and system for growing and maintaining an optimized/ideal active yeast solution in the yeast tank and fermenter tank during the fermentation filling cycle are provided. A new yeast stage tank is used between the yeast tank and the fermenter tank allowing yeast to rapidly produce a huge amount of active young yeast cells for a fermenter during the filling period. A measurable and useful controlling factor, % DT/% Yeast by weight ratio (or “food” to yeast ratio), is used (e.g., % DT=glucose), which offers information on the health status of the yeast. The controlling factor is used to control the status of the yeast throughout the entire process.

A method for preparing 1,3-diacylglycerol by immobilizing Sn-2 lipase. The present application obtains the Sn-2 lipase adsorbed by the macroporous resin by adsorbing the Sn-2 lipase on the resin, cross-links and immobilizes the Sn-2 lipase, and obtains 1,3-diglycerol by one-step hydrolysis with the lipase. The method improves the utilization times, hydrolysis activity and specificity of the Sn-2 lipase during hydrolysis, and determines the optimal parameters by improving the experimental conditions. This makes up for the shortcomings of immobilization and realizes the one-step hydrolysis of 1,3-diacylglycerol. Under optimal conditions, the hydrolase activity of immobilized lipase CAL-A is 1937.86U/g, and the immobilization rate can reach 94.49%, and has good operational stability and storage stability. Secondly, the DAG content can reach 36.12%, which is obviously superior to the current existing technology, and significantly reduces the production cost and market value of 1,3-DAG, providing favorable value for the industrial production of immobilized enzymes.

A method for preparing 1,3-diacylglycerol by immobilizing Sn-2 lipase. The present application obtains the Sn-2 lipase adsorbed by the macroporous resin by adsorbing the Sn-2 lipase on the resin, cross-links and immobilizes the Sn-2 lipase, and obtains 1,3-diglycerol by one-step hydrolysis with the lipase. The method improves the utilization times, hydrolysis activity and specificity of the Sn-2 lipase during hydrolysis, and determines the optimal parameters by improving the experimental conditions. This makes up for the shortcomings of immobilization and realizes the one-step hydrolysis of 1,3-diacylglycerol. Under optimal conditions, the hydrolase activity of immobilized lipase CAL-A is 1937.86U/g, and the immobilization rate can reach 94.49%, and has good operational stability and storage stability. Secondly, the DAG content can reach 36.12%, which is obviously superior to the current existing technology, and significantly reduces the production cost and market value of 1,3-DAG, providing favorable value for the industrial production of immobilized enzymes.

The present invention relates to cellobiohydrolase variants and carbohydrate binding module variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

The present invention relates to cellobiohydrolase variants and carbohydrate binding module variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

The present invention relates to cellobiohydrolase variants and carbohydrate binding module variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

The present invention relates to cellobiohydrolase variants and carbohydrate binding module variants. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants.

The present invention relates to isolated polypeptides having laccase activity and polynucleotides encoding the polypeptides and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.