192 PATENT ABSTRACTS

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 /mug enzyme/minute at 55 degrees, pH 8.5 in 0.5 M Tris buffer without showing any substrate and/or product inhibition; (4) Reac- tivity: A broad spectrum serine type protease having activity at least 5 times greater than Lr~sin or chvmotrypsin towa_rd§ food grade proteins and bovine serum albumin; (5) Op- timum activity temperature and temperature range: The optimum activity temperature is 80 degrees C. at pH of 8.0 in 0.05 M Tris buffer at an ionic strength of 0.2 M NaCI; The temperature range is 35 degrees to 95 degrees 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 conditio~as and optimum ionic strength: The protease is tolerant to ionic strengths of from 0.0 to about 1.0 M NaC1; Optimum ionic strength is 0.2 M NaC1; (8) Isoelectric point: The isoelectric point is at an alkaline pH; and (9) Structure: The protease is a monomer.

5194382

M E T H O D F O R I N C R E A S I N G T H E E N Z Y M A T I C R E A C T I V I T Y O F

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

A process for making L-aminoacylase includes a cultivation of microorganism selected from a specy of Alcaligenes, especially the Alcaligenes denitrificans DA 181, and a separation of a pro- duced L-aminoacylase from the bacterial cells for obtaining the L-aminoacylase which may be further purified for the production of L-amino acid. The acylase made by such a process may have an increased stability, beneficial for its commercial and medical values.

5196312

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

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

Akira Miike, Toshio Tatano, Shizuoka, Japan assigned to Kyowa Medex Company Ltd

Disclosed is a method for determination of an activity of gamma-glutamyl transpeptidase, leucine aminopeptidase, alanine amino- peptidase, cystine aminopeptidase, X factor as a coagulation factor, thrombin, plasmin of plas- minogen series, kallikrein, chymotrypsin, alkali phosphatase, N-acetyl glucosaminase and amylase, by allowing a particular substrate to act on the enzyme to thereby form an enhancer; ox- idizing a chromogen by an oxidase in the pre- sence of the enhancer and oxygen to form a pigment; and determining the pigment. Also dis- closed is a test composition for carrying out the determination.

Rupert Herrmann, Hans-Joachim Guder, Mar- tina Junius-Comer, assigned to Boehringer Mannheim GmbH

In order to increase the enzymatic reactivity of beta-galactosidase, an azide, thiocyanate, cyanate and/or thiosulphate is added to the reac- tion mixture.

5194383

PROCESS FOR MAKING L- AMINOACYLASE

5196314

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

A C T I V I T I E S

Michael-Harold Town, Joachim Siedel, Joachim Ziegenhorn, Shizuoka, assigned to Boehringer Mannheim GmbH

Ying C Tsai, Hsiang L Hu, Yunn B Yang, as- signed to National Science Council of Republic of China

A process for the determination of substrate or enzyme activities by the use of a redox reaction as a measurement reaction is carried out in the

PATENT ABSTRACTS

presence of one or more additionally added tetrazolium salts to remove disturbing sub- stances. The tetrazolium salts have the formula See Patent for Chemical Structure (I) in which R1 is a hydrogen atom, a carboxyl group or an alkyl, phenyl, nitrophenyl, dinitrophenyl, carboxyl- substituted phenyl or trialkylammoniumphenyl radical, R2 is a phenyl, nitrophenyl, biphenylyl or naphthyl radical, R3 is a phenyl, carboxyl- substituted phenyl, carboxyl-substituted hydro- xyphenyl or dimethylthiazolyl radical, and A negative earth is a monovalent anion. The for- mazanes formed by reaction with reducing sub- stances do not absorb light at all, or absorb light only to a negligible extent, at the measurement wavelength of the redox reaction. New com- pounds included within the structural formula are those in which RI is earboxy, phenyl, 2- carboxyphenyl, 4-carboxyphenyl, 2,4- dinitrophenyl or 4-trimethylammoniumphenyl, R2 is phenyl, and R3 is phenyl or 2- earboxyphenyl; with the proviso that, when R3 is unsubstituted phenyl or 2-carboxyphenyl, R1 may not be unsubstituted phenyl.

5196316

E N Z Y M E A N D D N A C O D I N G T H E R E F O R

Yasuno Iwasaki, Yoshik Nishikawa, Takarazuka, Japan assigned to Japat Ltd

The invention concerns a peptidylhydroxygiy- cine N-C lyase (PHL) catalyzing the reaction See Patent for Tabular Presentation PS wherein R represents a peptide residue, and GIyOH represents an alpha-hydroxyglycine residue linked to the C-terminus of said pcptide R by an amide bond, a recombinant DNA molecule coding for a PHL, a method for the preparation of such a recombinant DNA molecule, processes for the preparation of PHL from a natural source or by means of the said recombinant DNA molecule, and the use of PHL for the pre- paration of an amidated peptide R-NH2.

5196340

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

S E P A R A T E L A Y E R S O F A M E M B R A N E

Shigeyuk Miyamoto, Tokyo, Japan assigned to NEC Corporation

193

An enzyme electrode comprising an enzyme and a coenzyme immobilized in at least one layer is provided. This electrode has an outer membrane preventing the coenzyme from dissipation and so sensitivity and durability can be improved. In an inner membrane containing the enzyme and the cocnzyme, a mediator of electron transfer may be added. The enzyme and the cocnzyme may be separated in two layers, respectively, in the inner membrane to improve measurement sensitivity.

5198353

METHOD FOR PREPARING STABILIZED ENZYME

DISPERSION

John Hawkins, Philip Chadwick, Edward T Messenger, Mads Lykke, Tokyo, assigned to Novo Nordisk A/S; Albright & Wilson Limit

Disclosed is a method for preparing a stabilized enzyme dispersion wherein the dispersion is pre- pared by precipitating a water-soluble polymer from a single phase, aqueous solution to form an aqueous dispersion, and before, simultaneously with or after precipitating the polymer, con- tatting the dissolved or dispersed polymer with an aqueous solution or fine aqueous dispersion of an enzyme without any covalent bonding bet- ween the polymer and the enzyme. Also disclosed is a clear solution for use in the method.

5198355

P U R I F I C A T I O N O F G L Y C O S A M I N O G L Y C A N

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

Hiroshi Kikuchi, Ken-ich Maeyama, Keiichi Yoshida, Tokyo, assigned to Seikagaku Kogyo Co Ltd

Glycosaminoglycan degrading enzymes are fractionated and purified by chromatographically treating a solution con- mining the enzymes with an insoluble sulfated polysaccharide carrier. The enzymes are adsor- bed onto the carrier and then subsequently des- robed from the carrier.