Abstract: The present disclosure relates to an enzyme blend comprising a low pH, thermostable alpha-amylase and a Bacillus licheniformis alpha-amylase. The blend can include at least about 1.0 Liquefon Unit (LU) of the B. licheniformis alpha-amylase for every 5.0 Modified Wohlgemuth Unit (MWU) of the low pH, thermostable alpha-amylase. The enzyme blend described is suitable for starch liquefaction and saccharification, ethanol production, and/or sweetener production, among other things. Also provided herein is a method of processing a starch by liquefying the starch with the low pH, thermostable alpha-amylase and the Bacillus licheniformis alpha-amylase, simultaneously or sequentially.

Abstract: The present disclosure relates to an enzyme blend comprising a low pH, thermostable alpha-amylase and a Bacillus licheniformis alpha-amylase. The blend can include at least about 1.0 Liquefon Unit (LU) of the B. licheniformis alpha-amylase for every 5.0 Modified Wohlgemuth Unit (MWU) of the low pH, thermostable alpha-amylase. The enzyme blend described is suitable for starch liquefaction and saccharification, ethanol production, and/or sweetener production, among other things. Also provided herein is a method of processing a starch by liquefying the starch with the low pH, thermostable alpha-amylase and the Bacillus licheniformis alpha-amylase, simultaneously or sequentially.

Abstract: The present disclosure relates to an enzyme blend comprising a low pH, thermostable alpha-amylase and a Bacillus licheniformis alpha-amylase. The blend can include at least about 1.0 Liquefon Unit (LU) of the B. licheniformis alpha-amylase for every 5.0 Modified Wohlgemuth Unit (MWU) of the low pH, thermostable alpha-amylase. The enzyme blend described is suitable for starch liquefaction and saccharification, ethanol production, and/or sweetener production, among other things. Also provided herein is a method of processing a starch by liquefying the starch with the low pH, thermostable alpha-amylase and the Bacillus licheniformis alpha-amylase, simultaneously or sequentially.

Abstract: The present disclosure relates to an enzyme blend comprising a low pH, thermostable alpha-amylase and a Bacillus licheniformis alpha-amylase. The blend can include at least about 1.0 Liquefon Unit (LU) of the B. licheniformis alpha-amylase for every 5.0 Modified Wohlgemuth Unit (MWU) of the low pH, thermostable alpha-amylase. The enzyme blend described is suitable for starch liquefaction and saccharification, ethanol production, and/or sweetener production, among other things. Also provided herein is a method of processing a starch by liquefying the starch with the low pH, thermostable alpha-amylase and the Bacillus licheniformis alpha-amylase, simultaneously or sequentially.

Abstract: Biologically active lymphotoxin polypeptides are synthesized in recombinant cell culture. Novel nucleic acid and vectors incorporating same are provided. The compositions and processes herein enable the economical preparation of compositions containing uniform lymphotoxin polypeptides and variant lymphotoxins having amino acid sequences that differ from those found in nature. The lymphotoxins are purified to a specific activity of 2-10×107 units/mg of protein by purification using a novel immobilized, lymphotoxin-neutralizing monoclonal antibody.

Abstract: Biologically active lymphotoxin polypeptides are synthesized in recombinant cell culture. Novel nucleic acid and vectors incorporating same are provided. The compositions and processes herein enable the economical preparation of compositions containing uniform lymphotoxin polypeptides and variant lymphotoxins having amino acid sequences that differ from those found in nature. The lymphotoxins are purified to a specific activity of 2-10.times.10.sup.7 units/mg of protein by purification using a novel immobilized, lymphotoxin-neutralizing monoclonal antibody.

Abstract: Biologically active lymphotoxin polypeptides are synthesized in recombinant cell culture. Novel nucleic acid and vectors incorporating same are provided. The compositions and processes herein enable the economical preparation of compositions containing uniform lymphotoxin polypeptides and variant lymphotoxins having amino acid sequences that differ from those found in nature. The lymphotoxins are purified to a specific activity of 2-10.times.10.sup.7 units/mg of protein by purification using a novel immobilized, lymphotoxin-neutralizing monoclonal antibody.

Abstract: Human HL-60 lectin having an amino acid sequence different from other known animal lectins is disclosed. This is one member of a class of mammalian lectins extractable in lactose or detergent and specific for beta-D-galactosides (14-beta-gal lectin which contains at least one glycosylation site). Recombinant methods and materials for production of the mammalian 14-beta-gal lectins, especially HL-60 lectin, in a variety of hosts, and methods to utilize the resulting lectins are also described. Human HL-60 lectin is found in HL-60 cells and in placental tissue.