Abstract: A novel protease product suitable for admixture to washing compositions and exhibiting substantially attenuated allergenic properties is prepared by cultivating strains of Bacillus licheniformis which have been mutated to block their synthesis of protease other than Subtilopeptidase A (subtilisin). The commercial Bacillus licheniformis derived protease products are mixtures of subtilisin and a non-serine protease of lower stability and greater allergenicity than subtilisin.

Abstract: Saccharification of low DP polysaccharides of high glucose content syrups by short term contact with amyloglucosidase e.g. 1-10 hours, 1-10 AG units/gm of syrup solids, and syrup concentrations of 5-25 w/o solids in a batch saccharification, less than 30 minutes in a continuous process employing immobilized AMG.Suitable high glucose content syrups are co-products that result from fractionation of isosyrup into 50+% d.s.b. fructose syrups and from production of crystalline dextrose.

Abstract: Saccharification of low DP polysaccharides in syrups of high fructose content and low glucose content by short term contact with amyloglucosidase e.g. in less than 60 minutes, 1-10 AG units/gm of syrup solids, and syrup concentrations of 2-50 w/o solids in a continuous process employing immobilized AMG.Suitable high fructose content low glucose syrups are products that result from fractionation of isosyrup into enriched 50+% d.s.b. fructose syrups.

Abstract: A process for the preparation of penam and cephem derivatives by reacting a phosphite amide of a 6-aminopenicillanic acid or 7-aminocephalosporanic acid with an acyl halide in an aprotic solvent in the presence of a phosphite halide scavenger.

Abstract: p-Trimethylsilyloxy-D-(-)-phenylglycyloxysuccinimide or -phthalimide, process of preparing p-trimethylsilyloxy-D-(-)-phenylglycyloxysuccinimide or -phthalimide by reacting D-(-)-p-trimethylsilyloxyphenylglycin-N-carboxyanhydride with a N-hydroxyimide, and process for preparing 6-(p-hydroxyphenylglycylamido)-penam or 7-(p-hydroxyphenylglycylamido)-cephem compounds by reacting p-trimethylsilyloxy-D-(-)-phenylglycyloxysuccinimide or -phthalimide with a phosphite amide or an ester of 6-aminopenicillanic acid or of an ester of a 7-amino-3-cephem-4-carboxylic acid in the presence of the hydrochloride of a weak amine.

Abstract: Iron activation of cell mass of glucose isomerase preparations carried out by direct incorporation of 0.05-2.0% w/w dry basis of iron as a solid water soluble non-toxic iron salt.Preferred compositions are dry state particulate glucose isomerases containing 0.05-2.0% iron, 0.5-3.0% magnesium oxide, and 2-15% dextrose monohydrate all w/w.

Abstract: A system for collecting and stabilizing pasty material such as for example the mucosa available from slaughterhouse operations, employing a collecting tank, a storage reservoir and a preservative reservoir, the collecting tank being equipped with upper and lower liquid level controls and means associated with the controls so that when the pasty material accumulates to the level of the upper level control the pasty material is discharged to the storage reservoir and when the pasty material level thereafter drops to the position of the lower liquid level control, discharge is halted and preservative is metered from the preservative reservoir into the collecting tank.For cleaning out the collecting tank discharge can be continued until the collecting tank has been emptied. For startup a sensing element is provided at the bottom of the collecting tank to cause metering of preservative into the collecting tank when pasty material first enters the collecting tank.

Abstract: An immobilized saccharifying enzyme product formed by coating granular casein with a liquid-permeable proteinaceous layer comprising saccharifying enzyme and egg albumen cross-linked by reaction with glutaraldehyde.

Abstract: A beta-glucanase is prepared through the cultivation of Aspergillus phoenicis (Cda.) Thom or Aspergillus saitoi var Kagoshimaensis. This enzyme hydrolyzes the beta glucan of barley and can be employed to adjust the viscosity of wort and beer, through incorporation of the enzyme in mash or beer.

Abstract: Improved formation of enzyme granulates through inclusion within the composition of finely divided cellulose fibres.Optionally a waxy substance can be employed for the granulating agent, or to coat the granulate.

Abstract: Preparation of polypeptides from soy protein through hydrolysis with a microbial, alkaline, proteinase using enzyme concentrations of 4-25 Anson units per kg of soy protein, a substrate concentrtion of 5-20% w/w soy protein and pH 7-10, hydrolyzing to a (DH) degree of hydrolysis 8-15% then inactivating the enzyme by addition of a food grade acid, and thereafter recovering the supernatant polypeptide solution.Preferred are the proteinase from B. licheniformis, pH 7.5-8.5, 8-15% substrate, and hydrolysis to a DH 9.5-10.5 %.The product is free from bitterness.

Abstract: Modification of corn gluten by proteolytic hydrolysis, preferably by a microbial proteinase, of an aqueous corn gluten suspension substrate concentration above about 6% w/w based on protein dry matter with an enzyme concentration of 0.05 - 0.5 Anson units/liter. The hydrolysis being conducted until viscosity of the suspension exceeds about 50 cp., whereafter the enzyme is deactivated.Preferred proteinases are those derived from B. subtilis and B. licheniformis.The modified corn gluten is novel.

Abstract: An improvement in the conversion of penam and cephem compounds to secondary ammonium salts of phosphite amides thereof by reacting as follows: ##STR1## wherein --R, is the non-reacting balance of the penam or cephem compound and ##STR2## ARE NON-REACTING SUBSTITUENTS. Catalytic amounts of H--N< or the hydrogenhalide thereof may be present in the reaction medium.

Abstract: A method of producing enzyme preparations having L-.alpha.-amino acyl amidase activity comprising cultivating a micro-organism selected from the group consisting of Pseudomonas putida, Pseudomonas reptilivora, and Pseudomonas arvilla in a nutrient medium and separating an enzyme preparation from said nutrient medium.A process of preparing L-.alpha.-amino acid and D-.alpha.-amino acid amide from DL-.alpha.-amino acid amide by contacting said DL-.alpha.-amino acid amide with an enzyme preparation obtained by cultivating a micro-organism selected from the group consisting of Pseudomonas putida, Pseudomonas reptilivora, and Pseudomonas arvilla in the presence of a nutrient medium and separating the L-.alpha.-amino acid and D-.alpha.-amino acid amide thus formed.

Abstract: In the treatment of collagen containing materials for gelatin extraction purposes, conditioning the collagen source enzymatically at pH 7-13 with protease, pH level being selected to match the pH optimum of the protease, for 4-72 hours, at 20.degree. - 40.degree. C.

Abstract: Conversion of penicillin sulfoxides to the corresponding 3-desacetoxycelphalosporins are carried out in high yield by heating, e.g. 80.degree.-130.degree. C, a solvent solution of the penicillin in the presence of a complex formed by a phosphite or phosphine amide with the salt of a strong acid and a nitrogenous base, e.g. alpha-picoline hydrobromide.One preferred amide is 2-piperidino-1,3,2-dioxaphospolane.

Abstract: Production of glucose isomerase from facultative aerobic microorganisms by limiting oxygen supply to growth-limiting amounts in the presence of excess glucose and other nutrients in sufficient amounts.Enzyme yield from oxygen growth-limiting proportions is superior to yields obtained from glucose growth-limiting circumstances.

Abstract: Continuous enzymatic isomerization of a glucose syrup with a glucose concentration of 30-55% by weight containing less than about 10.sup.-.sup.3 M calcium, less than about 10.sup.-.sup.2 M of Mg.sup.+.sup.+, the Mg.sup.+.sup.+ being in a concentration, whereby the molar ratio of magnesium to calcium is greater than 5, the isomerization taking place at a pH 7.8-8.6 with a total contact time between enzyme and syrup less than about 3.5 hours, preferably less than 2 hours. A convenient temperature range for isomerization is 60.degree.-85.degree. C., preferably 60.degree.-70.degree. C. The syrup has no colbalt added thereto. A preferred practice involves a syrup with very little added magnesium. Post isomerization ion exchange treatment can be avoided.The enzyme is a particulate preparation derived from B. coagulans, preferably by glutaraldehyde reaction with homogenized microorganism cells.

Abstract: Saccharification of 10-20% solid content dextrin solutions for 15-75 hours at amyloglucosidase enzyme dosage levels of 0.3-1.0 AG u/g of solids results in glucose syrups with purity levels exceeding 98%.Glucose purity levels in excess of 98.5% can be achieved if the dextrin solution is formed by enzymatic liquefaction of starch, and saccharification is carried out for 15-25 hours with 0.4-0.8 AG u/g.

Abstract: Method of recovering high purity cephalexin in high yields from a solution containing cephalexin comprising the steps of reacting said solution with a non-substituted or substituted naphthalene to form a complex with cephalexin, isolating said complex, and decomposing said complex to recover cephalexin or a salt thereof.