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Purification and Properties of Lactate Racemase from Lactobacillus Sake

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Purification and Properties of Lactate Racemase from Lactobacillus Sake The Journal of Biochemistry, Vol . 64, No. I, 1968 Purification and Properties of Lactate Racemase from Lactobacillus sake By TETSUG HIYAMA, SAKUzo FUKUI and KAKUO KITAHARA* (From the Institute of Applied Microbiology,University of Tokyo, Bunkyo-ku, Tokyo) (Received for publication, February 12, 1968) A lactate racemase [EC 5.1.2.1] was isolated and purified about 190 fold in specific activity from the sonic extract of Lactobacillus sake. The purified preparation was almost homogeneous by ultracentrifugal and electrophoretical analyses. Characteristic properties of the enzyme were as follows : (a) absorption spectrum showed a single peak at 274 my, (b) molecular weight was 25,000, (c) the enzyme did not require any additional cofactors and showed no activity of lactate dehydrogenase, (d) K, values were 1.7 •~ 10-2 M and 8.0 •~ 10-2 M for D and L-lactate, respectively, (e) optimal pH was 5.8-6.2, (f) an equilibrium point was at a molar ratio of 1/1 (L-isomer/D-isomer), (g) the enzyme activity was inhibited by atebrin, adenosine monosulfate, oxamate and some of Fe chelating agents, (h) pyruvate and acrylate were not incorporated into lactate during the reaction, and (i) exchange reaction of hydrogen between lactate and water did not occur during the reaction. Since the first observation on the enzy the addition of both NAD and pyridoxamine matic racemization of optical active lactate phosphate. In this paper we deal with the by lactic acid bacteria had been reported by purification and properties of the lactate KATAGIRI and KITAHARA in 1936 (1), racemases racemizing enzyme from the cells of L. sake. for various substances were successively disco vered in various organisms (2-8), and their MATERIALS AND METHODS physiological significance and reaction me Organism and Cultivation-Lacobacillus sake 012 chanism were discussed. which was isolated from sake starter in our laboratory On the biochemical racemization of lac was used. The bacterium was cultured at 30•Ž under tate, following two systems were presented : static condition in a medium containing 2 g of yeast one is lactate racemase [EC 5.1.2.1] in extract (Daigo Eiyo-Kagaku Co. Ltd., Osaka), lO g Clostridium (9, 10) and another is the coupl of Ehlrich's meat extract, 10 g of polypeptone (Daigo) ing system of NAD linked D and L-lactate and 15 g of glucose per liter. The medium was dehydrogenases [EC 1. 1.1.28 and 1. 1.1.27] in adjusted to pH 7.0 with KOH and sterilized at 120•Ž Lactobacillus (11). The former requires pyrido for 10 min. First seed culture was performed in 10 ml xamine-phosphate and ferrous ion as cofactors of the medium by 20 hr cultivation. To prepare and does not include any activity of lactate second seed culture, whole volume of the first seed dehydrogenase. culture was inoculated into 2 liters of the medium, and cultivation was carried out for 20 hr. Three Recently, we found that the racemase hundred milliters of the second seed culture was ino activity in Lactobacillus sake is not affected by culated into each of six Erlenmeyer flasks contain * Present address: Tokyo University of Agricul ing 10 liters of the medium per flask. The culture, ture, Tokyo. total volume of 60 liters, was incubated for 20 hr. 99 100 T . HIYAMA, S. FUKUI and K. KITAHARA After the cultivation , the cells were harvested by hydrolyzed before use. Adenosine monosulfate (Na centrifugation and washed twice with 0 .5% NaCl and salt) was kindly supplied by Dr. M. Ishimoto, Universi finally with distilled water . The cells thus obtained ty of Hokkaido. were stored at -20•Ž . During the storage for a Other chemicals were commercial products. month any loss in the enzyme activity was not observed. From 60 liters culture , 12g of dry cells RESULTS were obtained . Purification of Lactate Racemase-All opera Assay of Lactate Racemase-Assay system for lactate racemase contained 10 ƒÊmoles of sodium D-lactate or tions were carried out at 4•Ž. Frozen cells, L-lactate, 20 ƒÊmoles of phosphate buffer 12 g dry weight, were suspended in deionized , pH 7.0, and racemase solution in a total volume of 0 .2 ml. The water to give a final volume of 200 ml. The reaction was carried out for 30 min at 30•Ž suspension was treated with sonic oscillation , then the mixture in a test tube was kept in boiling water for (10 kc, 100W) for 20 min to disrupt the cells. 30 sec to stop the reaction. An amount of optical Cell debris and intact cells were removed antipode formed from D or L-lactate was determined from the sonicated sample by centrifugation by the enzymatic methods of HIYAMA et al. (12) or at 25,000xg for 20 min. The supernatant was of HARN and BRUNS (13). The former is specific for incubated at 48•Ž for 3 min to precipitate D-lactate and the latter for L -lactate. One unit of heat-coagulable impurities. After removal of the enzyme is defined as an amount which con verts one ƒÊmole of L-lactate to D-isomer per hour precipitate by centrifugation, the supernatant was diluted with deionized water to 250 ml. under the conditions shown above. Specific activity To the diluted solution was added 62 g of is presented as an enzyme units per absorbance at 280mƒÊ. ammonium sulfate, and then the solution Determinaton of Metals-Metals in a racemase pre was allowed to stand for 2 hr. The precipitate paration were analyzed by atomic absorption spectrum formed was removed by centrifugation. To technique using a Hitachi-Perkin Elmer atomic absorp the clear supernatant obtained, further addi tion spectrophotometer. tion of 72 g of ammonium sulfate was per Separation of Lactic and Pyruvic Acids-Separation formed. The precipitate formed within 4 hr of lactic and pyruvic acids was carried out as follows : was collected by centrifugation at 10,000 •~ g a reaction mixture charged on a Dowex I •~ 8 (for for 10 min, and dissolved in deionized water mate type) column (I •~ 1 cm) was eluted successively of 21 ml. The solution was dialyzed overnight with 10 ml of 0.2 N and of 3.0 •~ formic acid. Lactic against one liter of deionized water, The and pyruvic acids were quantitatively recovered in dialyzate was kept at 50•Ž for 3 min. The the former and the latter eluates, respectively. By this procedure acrylic acid was not eluted from the precipitate formed by the treatment was re column. moved by ultracentrifugation at 105,000•~g Chemicals-D and L-lactic acids were prepared for 60 min. The supernatant was charged on from culture broths of Sporolactobacillusinulinus and a DEAE-cellulose column (3.5•~65 cm) equili Lactobacilluscasei, respectively. Lactic acid was ex brated with Mcllvaine buffer of 80 times tracted from the broth with ethyl ether. After dilution and pH 5.0. Elution was performed removal of ethyl ether from the extract , the acid with the same buffer containing 0.13m KCl was diluted with small amount of water and decolored at an elution rate of 7.0 ml per minute. The by passing through an activated carbon bed. The enzyme was recovered in tubes of number lactic acid was turned into zinc lactate by treatment 9-13 (each tube 200 ml). The enzyme solu with zinc carbonate. Zinc lactate was recrystallized twice from water. Purified free acid was prepared tion (1000 ml) was concentrated by dialysis against flakes of polyethylenglycol (Tpye 6000 from the lactate by passing through a cation ex , D changer resin column. Lactic acid obtained was ainippon Seiyaku Co. Ltd., Osaka) for 10 hr. neutralized with NaOH and then used as substrate The concentrated sample (10 ml) was diluted for lactate racemase. with deionized water to decrease ionic strength . Pyruvic acid (3-14C) and tritiated water were Then, the sample was applied to a second purchased from the Radiochemical Centre, England. column chromatography of DEAE-cellulose Acrylate methyl ester (2, 3-14C) was obtained from (1 •~ 15 cm) which was pretreated with the Nuclear Research Chemicals, Inc., U.S.A., which was same buffer of McIlvaine mentioned above . Lactate Racemase 101 TABLE I Purification of lactate racemase. FIG. 1. Sedimentation patterns of lactate racemase. Ultracentrifugation was performed with the purified enzyme dissolved in 0.5m KC1, pH 5.0, in a Hitachi ultracentrifuge. Protein concentra tion was 1.7 mg per ml. Experimental conditions were as follows : temperature, 18•Ž; speed, 59,400 rpm ; bar angle, 55ß; pictures on the left and right were obtained after 28 and 48 min of centrifugation, respectively. Elution was also carried out in the same manner as presented above. Fractions giving high specific activity (tube number 7-13, each tube 10 ml) were collected and dialyzed against deionized water for 4 hr. The dialyzed preparation (120 ml) was charged on a DEAE FIG. 2. Electrophoretical pattern of lactate cellulose column (1 •~ 2 cm) buffered with the racemase. same concentration of Mcllvaine buffer in Electrophoretical pattern was obtained by the above, then the enzyme adsorbed was disc electrophoresis under the conditions of eluted with 2.0 ml of 0.5 Nt KCl. The enzyme ORNSTEIN and DAVIS (14) preparation obtained was concentrated 190 . The final preparation was used in the follow fold in specific activity. Whole procedure of ing sections for enzymatic study. the purification is summarized in Table I. 102 T. HIYAMA, S. FUKUI and K. KITAHARA Patterns in Ultracentrifugation and Electro molecular weight 12,600, Sankyo Co. Ltd., phoresis-Asedimentation pattern of the enzyme Tokyo) bovine serum albumin (assigned M.W., is shown in Fig.
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