Enzymes and Enzyme Systems

5160418

ENZYME ELECTRODES AND IMPROVEMENTS IN THE

MANUFACTURETHEREOF

5162203

METHODS OF MEASURING ISOZYMES AND ISOZYME

CLASSES OF ALCOHOL DEHYDROGENASE

William Mullen, Ely, United Kingdom assigned to Cambridge Life Sciences plc

Enzyme electrodes are disclosed consisting es- sentially of a uniform homogeneous layer of a finely divided platinum group metal or oxide, preferably preadsorbed onto the surface of an activated carbon or grapite powder, and deposited from suspension upon the surface of an electrically conductive substrate and in ad- mixture with an enzyme and optionally a water soluble or water-dispersible binder. Preferably the enzyme electrodes are produced by coating the substrate with a suspension of the enzyme, the finely divided platinum group metal, and if present the carbon or graphite powder and bi- nder, and drying at a temperature below that at which the enzyme is deactivated.

5160525

BIOREMEDIATION ENZYMATIC COMPOSITION

Neil W Stillman, Edward J Brown

A chemical product and method for accelerated biodegradation of petroleum on water. The chemical product includes a fermentation pro- duct portion and a surfactant containing em- ulsifier portion which has a monosodium glutamate additive.

Bert L Vallee assigned to President and Fellows of Harvard College

The present invention provides fluorescence- based methods for sensitively detecting total ADH activity in human sera and selectively measuring the activity of different classes of ADH in human sera and other body fluids and tissues. The present invention also provides highly purified Class 1, Class II, and Class III isozymes, and methods for their purifiation. The class of substrates consisting of various naphthaldehydes and quinoline aldehydes pro- vide the requisite sensitivity and selectivity for measurements of the activity of ADH and in- dividual ADH classes. These fluorescence-based methods may serve as a diagnostic aid in disease assessment, in particular, diagnosis of alcohol abuse, alcoholism, alcohol consumption, altered alcohol sensitivity or tolerance.

5162210

PROCESS FOR ENZYMATIC HYDROLYSIS OF STARCH TO

GLUCOSE

Michael Sierks, Birte Svensson assigned to Iowa State University Research Foundation

A process for converting starch or partially hydrolyzed starch into a syrup containing dex- trose includes the steps of saccharifying starch hydrolyzate in the presence of a saccharifying starch hydrolyzate in the presence of a mutated glucoamylase or related enzyme and increasing the selectivity of the enzyme for alpha-(1 right arrow4)-glucosidic bonds by the glucoamylase or related enzyme by including at least one muta- tion, the mutation substituting an amino acid of

155

156 PATENT ABSTRACTS

the enzyme with at least one amino acid chosen by comparison with structurally related regions of other enzymes that selectively hydrolyze only alpha-(1 right arrow4) glucosidic bonds. En- zymes made in accordance with the present in- vention are also disclosed.

5162221

F R U C T O S E - l , 6 - B I S P H O S P H A T E A L D O L A S E , A P R O C E S S F O R

T H E P R E P A R A T I O N T H E R E O F A N D I T S U S E

Hans-Peter Brockamp, Maria-Regina Kula, Friedrich Goetz, Niederzier, Federal Republic Of Germany assigned to Forschungszentrum Juelich GmbH

A fructose-l,6-bisphosphate aldolase with ob- tained from Staphylococcus carnosus is dis- closed, The aldolase has considerably improved stability as compared to aldolase from rabbit muscle, having an inactivation rate of 0.77%/d at 25 degrees C. as compared with 59.3%/d for rab- bit muscle aldolase. The aldolase is obtained by culturing Staphylococcus carnosus cells, mechanically disrupting the cell mass, and then working up the product by fractional am- monium sulfate precipitation, pH fractionation and ion exchange chromatography to provide F- 1,6-BP aldolase with a specific activity of 25 U/mg in 21% yield. Particularly high yields are obtained by the aqueous 2-phase extraction and obtaining the enzyme from the upper phase by anion exchange chromatography. The aldolase is suitable for synthesis of carbohydrates and derivatives thereof by enzymatic reaction of al- dehydes with DHAP.

5164311

P R E P A R A T I O N O F A N A N T I B O D Y - E N Z Y M E

C O N J U G A T E

Ravinder K Gupta assigned to Coulter Corpora- tion

An antibody-enzyme conjugate is prepared having an enzyme to antibody ratio of approx- imately 3. The conjugate is produced by adding sulfhydryl groups to an antibody and maleimidyl groups to an enzyme to produce a modified anti- body and enzyme, and reacting the modified antibody and enzyme to produce the conjugate. In producing the modified antibody and enzyme, about a 15 molar excess of reagents for in- troducing sulfhydryl and maleimidyl groups is used. When reacting the modified antibody and enzyme, a four molar excess of the modified en- zyme is used, and reacting is stopped after a specified period of time by addition of selective reagents. The selective reagents may be cysteine and iodoacetamide.

5164312

M E T H O D F O R S T A B I L I Z I N G T H E E N Z Y M E L A C T O P E R O X I D A S E I N

P R O D U C T S

Karl E L Bjorck, Uppsala, Sweden assigned to Ewos Aktiebolag

The present invention relates to a method for ob- taining an increased stability at storage of the en- zyme lactoperoxidase in particularly dry products, as well as such products, whereby the hydrogen ion concentration is adjusted to 10- 3.25-10-6,

5164181

E N Z Y M E C A S T R A T I O N O F A N I M A L S

Jule Silver, Robert E Hopkins assigned to Robert E Hopkins II D V M Inc

Male animals may be chemically castrated by in- jecting both testes and/or both spermatic cords with a castratingly effective amount of a pro- tease enzyme such as a chymopapain-rich enzyme preparation.

5164318

A U T O M A T I C E N Z Y M E I M M U N O A S S A Y A N A L Y Z E R

Takeshi Sato, Tomonori Mimura, Katsuta, Japan assigned to Hitachi Ltd

A sample containing a non-labeled antibOdy (or a non-labeled antigen) is drawn into a probe having contained therein an antigen (or an anti- body) to which a labeled antibody (or a labeled antigen) is bound. A competitive reaction takes place in the probe. The amount of the non-