Cornell University

Sandoz Gmbh

Novartis Ag

Shriners Hospitals for Crippled Children

J. Wesley Alexander

Vigen K. Babayan

Mitchell T. Gersovitz

Jerome J. Licari

Frederick Rudolph

Frank B. Cerra

Novartis Nutrition Inc.

John E. Kinsella

Charles T. Van Buren

George L. Blackburn

John M. Daly

John E Kinsella

Jayarama K Shetty

John T Daly

George L Blackburn

Vigen K Babayan

Jerome J Licari

J Wesley Alexander

Charles T Van Buren

David B Wilson

Frank B Cerra

Mitchell T Gersovitz

Todd W Gusek

Chee H Tsai

Damodaran Srinivasan

John M Daly

The invention provides immunostimulatory compositions comprising an aggregate immunostimulatory amount of

Compositions and methods for the enhancement of host defense mechanisms

An exocellular protease from Thermomonospora fusca YX and a process for producing the protease which has the following physicochemical properties: (1) Molecular mass: The protease has a molecular mass of from about 10,000 to 14,000 Daltons as measured by SDS-polyacrylamide gel electrophoresis; (2) Influence of inhibitors: The protease activity is inhibited by serine protease inhibitors; (3) Substrate specificity: A non-specific protease which can hydrolyze food proteins and bovine serum albumin at a rate of 50-100 nmoles peptide bonds/.mu.g enzyme/minute at 55.degree., pH 8.5 in 0.5 M Tris buffer without showing any substrate and/or product inhibition; (4) Reactivity: A broad spectrum serine type protease having activity at least 5 times greater than trypsin or chymotrypsin towards food grade proteins and bovine serum albumin; (5) Optimum activity temperature and temperature range: The optimum activity temperature is 80.degree. C. at pH of 8.0 in 0.05 M Tris buffer at an ionic strength of 0.2 M NaCl; The temperature range is 35.degree. to 95.degree. C. under the same pH, buffer, and ionic strength; (6) pH range and optimum pH value: The protease has a pH activity range of from about 7 to 11, and the optimum pH value is 9.0; (7) Tolerance to ionic strength conditions and optimum ionic strength: The protease is tolerant to ionic strengths of from 0.0 to about 1.0 M NaCl; Optimum ionic strength is 0.2 M NaCl; (8) Isoelectric point: The isoelectric point is at an alkaline pH; and (9) Structure: The protease is a monomer.

Alkali and heat stable protease from thermomonospora fusca

The present invention comprises a process for treating nucleoprotein complexes with a chaotropic salt in order to dissociate the nucleic acids from the nucleo-protein complexes, and then isoelectrically precipitating a nucleic acid diminished protein containing fraction from a nucleic acid enriched supernatant.

Method for separation and recovery of proteins and nucleic acids from

The present invention relates to a process which comprises recovering proteinaceous materials from nucleoprotein complexes by derivatizing the proteinaceous material with a cyclic anhydride, thereby disassocating the complex, separating the derivatized proteinaceous material from the nucleic acids and subsequently regenerating the proteinaceous material. The recovery of the proteinaceous material is accomplished by maintaining the separated derivatized proteinaceous material at a suitable acidic pH, which is a function of the reaction time and the temperature, until the derivatized proteinaceous material is disassociated into the proteinaceous material and the cyclic anhydride or most usually the equivalent acid and the proteinaceous material is recovered.

Recovery of proteinaceous material having reduced nucleic acid levels

The invention relates to culturing cocoa bean cells in the presence of a cocoa bean cell culture growth supporting medium for a time and at a temperature sufficient to produce a metabolite, e.g. triglyceride species similar to those normally found in cocoa butter and isolating said metabolite.

Cocoa bean cell culture

The process of the invention comprises disrupting microbial protein containing cells; derivatizing the resultant mixture comprising protein and nucleic acid with an acid anhydride; and then isoelectrically precipitating a nucleic acid diminished protein containing fraction from a nucleic acid enriched supernatant.

Anhydride modified microbial protein having reduced nucleic acid levels

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Ithaca, NY, United States of America

John E Kinsella