326 PATENT ABSTRACTS

of the aromatic amino acid biosynthesis path- way, is imparted to a glyphosate sensitive host. A mutated aroA gene is employed which expresses 5-enolpyruvyl-3-phosphoshikimate synthetase (EC: 2.5.1.19) (ES-3-P synthetase). Methods are provided for obtaining the aroA mutation which provides the enzyme resistant to inhibition by glyphosate, means for introducing the structural gene into a sensitive host, as well as providing a method of producing the enzyme. The E. coli strain C600(pPMGI) has been deposited at the A.T.C.C. on Dec. 14, 1982 and been given A.T.C.C. accession no. 39256.

4 5 3 ~ 7 7

T H E R M O S T A B L E G L U C O A M Y L A S E A N D M E T H O D

F O R I T S P R O D U C T I O N

4540668

A L C O H O L O X I D A S E F R O M P I C H I A - T Y P E Y E A S T S

Thomas R Hopkins assigned to Phillips Petro- leum Company

A new alcohol oxidase is isolated from Pichia- type microorganisms in soluble or crystalline form. The crystalline novel enzyme is isolated by preparing an aqueous fluid containing cells of a Pichia-type microorganism, homogenizing the fluid and separating solids therefrom to produce an alcohol oxidase solution, adjusting the solu- tion to have an ionic strength in the range of 0.05 to 0.01 in ionic strength to form a recovery range solution thereby causing the crystalline alcohol oxidase to form. The new enzyme is used to determine alcohol concentrations in fluid sam- ples in which conditions are compatible with the enzyme's activity.

Dennis M Katkocin, Nancy S Word, Shiow- Shon Yang assigned to CPC International Inc

This invention relates to a glucoamylase enzyme exhibiting thermostability at pH values between 6 and 7 which is derived from a spore-forming, thermophilic, anaerobic bacterium and to a pro- cess for its production. The glucoamylase is espe- dally useful for the preparation of glucose- containing syrups from starch.

4542098

P R O D U C T I O N O F G L U C O S E D E H Y D R O G E N A S E A N D U S E O F

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

L - C A R N I T I N E

Jean-Paul Vandecasteele, Daniel BaUerini, Jeanine Lemal, Yann Le Penru, Fourqueux, France assigned to Institut Francais du Petrole

4537764

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

B - D - G L U C O S E A N D G L U C O S E O X I D A S E

Michael A Pellico, Robert Montgomery as- signed to Laclede Professional Products Inc

An enzymatic dentifrice is provided which con- tains an enzyme system comprising Beta-D- glucose and glucose oxidase for producing hydrogen peroxide upon oral application of the dentifrice. The enzymatic dentifrice is stabilized against the production of hydrogen peroxide prior to oral application of the dentifrice by limiting any water in the dentifrice to an amount not more than about 10 wt. % based on the weight of the dentifrice.

A process for producing glucose dehydrogenase consists of cultivating a mutant strain (ATCC 39 118) of Bacillus megaterium in a culture medium and recovering the resultant glucose dehy- drogenase. The latter can be used in the en- zymatic production of L-carnitine consisting of subjecting 3-dehydrocarnitine to the simul- taneous action of carnitine dehydrogenase, nicotinamide adenine dinucleotide and glucose and glucose dehydrogenase.

4542099

M E T H O D F O R M A N U F A C T U R I N G R E S T R I C T I O N

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

Toshizo Sakurai, Toshiyuki Kosaka, Tokyo, Japan assigned to Kabushiki Kaisha Yakult Honsha