JPH0349693A - Production of n-acetyllactosamine - Google Patents
Production of n-acetyllactosamineInfo
- Publication number
- JPH0349693A JPH0349693A JP18491989A JP18491989A JPH0349693A JP H0349693 A JPH0349693 A JP H0349693A JP 18491989 A JP18491989 A JP 18491989A JP 18491989 A JP18491989 A JP 18491989A JP H0349693 A JPH0349693 A JP H0349693A
- Authority
- JP
- Japan
- Prior art keywords
- acetyllactosamine
- acetylglucosamine
- galactosidase
- lactose
- reaction solution
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- KFEUJDWYNGMDBV-UHFFFAOYSA-N (N-Acetyl)-glucosamin-4-beta-galaktosid Natural products OC1C(NC(=O)C)C(O)OC(CO)C1OC1C(O)C(O)C(O)C(CO)O1 KFEUJDWYNGMDBV-UHFFFAOYSA-N 0.000 title claims abstract description 20
- KFEUJDWYNGMDBV-LODBTCKLSA-N N-acetyllactosamine Chemical compound O[C@@H]1[C@@H](NC(=O)C)[C@H](O)O[C@H](CO)[C@H]1O[C@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 KFEUJDWYNGMDBV-LODBTCKLSA-N 0.000 title claims abstract description 20
- HESSGHHCXGBPAJ-UHFFFAOYSA-N N-acetyllactosamine Natural products CC(=O)NC(C=O)C(O)C(C(O)CO)OC1OC(CO)C(O)C(O)C1O HESSGHHCXGBPAJ-UHFFFAOYSA-N 0.000 title claims abstract description 20
- 238000004519 manufacturing process Methods 0.000 title claims description 8
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 claims abstract description 11
- 229950006780 n-acetylglucosamine Drugs 0.000 claims abstract description 11
- 108010005774 beta-Galactosidase Proteins 0.000 claims abstract description 10
- 239000000758 substrate Substances 0.000 claims abstract description 10
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 claims abstract description 9
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 claims abstract description 9
- MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 claims abstract description 9
- 102000005936 beta-Galactosidase Human genes 0.000 claims abstract description 9
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 9
- 239000008101 lactose Substances 0.000 claims abstract description 9
- 238000005185 salting out Methods 0.000 claims abstract description 8
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 claims abstract description 5
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims abstract description 5
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims abstract description 5
- 235000011130 ammonium sulphate Nutrition 0.000 claims abstract description 5
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 claims description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 4
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 claims description 4
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 claims description 2
- 229910052943 magnesium sulfate Inorganic materials 0.000 claims description 2
- 235000019341 magnesium sulphate Nutrition 0.000 claims description 2
- 229910000160 potassium phosphate Inorganic materials 0.000 claims description 2
- 235000011009 potassium phosphates Nutrition 0.000 claims description 2
- 239000011780 sodium chloride Substances 0.000 claims description 2
- 235000002639 sodium chloride Nutrition 0.000 claims description 2
- 239000001509 sodium citrate Substances 0.000 claims description 2
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 claims description 2
- 235000011083 sodium citrates Nutrition 0.000 claims description 2
- 229910052938 sodium sulfate Inorganic materials 0.000 claims description 2
- 235000011152 sodium sulphate Nutrition 0.000 claims description 2
- 238000006243 chemical reaction Methods 0.000 abstract description 14
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 abstract description 3
- 238000004440 column chromatography Methods 0.000 abstract description 2
- 239000007795 chemical reaction product Substances 0.000 abstract 2
- 241000228245 Aspergillus niger Species 0.000 abstract 1
- 229910052799 carbon Inorganic materials 0.000 abstract 1
- 108090000790 Enzymes Proteins 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 6
- 229940088598 enzyme Drugs 0.000 description 6
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 229930182830 galactose Natural products 0.000 description 3
- 229940068140 lactobacillus bifidus Drugs 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- DUKURNFHYQXCJG-UHFFFAOYSA-N Lewis A pentasaccharide Natural products OC1C(O)C(O)C(C)OC1OC1C(OC2C(C(O)C(O)C(CO)O2)O)C(NC(C)=O)C(OC2C(C(OC3C(OC(O)C(O)C3O)CO)OC(CO)C2O)O)OC1CO DUKURNFHYQXCJG-UHFFFAOYSA-N 0.000 description 2
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 2
- -1 amino disaccharide Chemical class 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 229920001542 oligosaccharide Polymers 0.000 description 2
- 150000002482 oligosaccharides Chemical class 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- IQUPABOKLQSFBK-UHFFFAOYSA-N 2-nitrophenol Chemical compound OC1=CC=CC=C1[N+]([O-])=O IQUPABOKLQSFBK-UHFFFAOYSA-N 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 101710155617 Beta-galactosidase 10 Proteins 0.000 description 1
- 241000186000 Bifidobacterium Species 0.000 description 1
- 241000510930 Brachyspira pilosicoli Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- 102000002464 Galactosidases Human genes 0.000 description 1
- 229930186217 Glycolipid Natural products 0.000 description 1
- 108010059881 Lactase Proteins 0.000 description 1
- 108010070158 Lactose synthase Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000006482 condensation reaction Methods 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000018044 dehydration Effects 0.000 description 1
- 238000006297 dehydration reaction Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 229940116108 lactase Drugs 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 210000000663 muscle cell Anatomy 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000006276 transfer reaction Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
Description
【発明の詳細な説明】
（産業上の利用分野〉
本発明は、大乳オリゴ糖や複合糖質の糖鎖中に含まれる
Ｎ−アセチルラクトサミンの製造法に関するものである
．
（従来の技術）
Ｎ−アセチルラクトサミンは、血液型糖蛋白質の分解物
から最初に単離されたガラクトースとＮ−アセチルグル
コサミンがβ一ｌ．４結合したアミノ２糖で、人乳才リ
ゴ糖や，ノボ多糖，各種の糖蛋白質及び糖脂質の糖鎖中
に存在する生化学的に非常に重要な才リゴ糖である．ま
た、腸肉細閑の一つビフィズス菌の発育因子としてち知
られ、機能性食品素材としても有用な物質である．
従来、Ｎ−アセチルラクトサミンの製造は一化学合成も
しくは高エネルギー化合物ＬＩＤＰ−ガラクトースとＮ
−アセチルグルコサミンを基質として、ラクトース合成
酵素により合成されることが知られているが、これらの
方法は，工程が複雑でしかも高価となり工業的にはまだ
難点の多い製造法である。一方，簡便な方法として、ラ
クトースとＮ−アセチルグルコサミンを基質として、ラ
クトバシラスビフィダス（Ｌａｃｔｏｂａｃｉｌｌｕｓ
ｂｉｆｉｄｕｓｌ やスボロボロミセス シングラリ
ス（Ｓ ｏｒｏｂｏｌｏｍｙｃｅ−ｓ 扛鳳虱トＢ）の
生菌体を用いた報告［Ｊ．Ｂｉ−ｏｌ．ｃｈｅｍ． ．
２１７．７９（１９５５） ．Ｃａｎ．Ｊ．Ｃｈｅｍ．
，４２，２３０７ （１９６４１ ］や、ラクトバシ
ラス ビフィダスの生産するβ−ガラクトシダーゼを作
用させた報告［ Ｊ． Ｒｉｏｔ． Ｃｈｅｍ． ．
２０８， ２９９ （１９５４） ］などがある．又、
最近ではガラクトースとＮ−アセチルグルコサミンを基
質としてエシエリシア コリ（ Ｅｓｃｈｅｒｉｃｈｉ
ａ ｃｏｌｉ）の生産するβ一ガラクトシダーゼを作用
させ、脱水縮合反応によるＮ−アセチルラクトサミン生
産の報告［第ｌＯ回糖質シンポジウム講演要旨集，ｐｉ
ｏ７＋ｔｃ＋ａ７） ］ち示されている．
〈発明が解決しようとする問題点〉
しかしながら、いずれの製造法もＮ−アセチルラクトサ
ミンの生成量が非常に少ない欠点がある．そこで本発明
者らは、前述の欠点を解決すべく種々検討した結果，ラ
クトースとＮ−アセチルグルコサミンを基質とし、β−
ガラクトシダーゼを塩析剤存在下で作用させることによ
り、Ｎ−アセチルラクトサミンの生成量が増加すること
を見い出し，本発明を完成するに至った．
〈問題を解決するための手段）
本発明は、ラクトースとＮ−アセチルグルコサミンを基
質とし、β−ガラクトシダーゼを虐析剤存在下で作用さ
せ、ガラクトース転移反応により、Ｎ−アセチルラクト
サミンを効率よく製造する方法を提供することを目的と
する．
本発明に用いるβ−ガラクトシダーゼとし−ａｃｉｌｌ
ｕｓ ｃｉｒｃｕｌａｎｓを起源とするものが例示でき
、これら市販されている酵素を使用することができる．
本発明の塩析剤としては、硫酸アンモニウム、硫酸ナト
リウム、リン酸カリウム、硫酸マグネシウム，クエン酸
ナトリウム，塩化ナトリウムが挙げられ、これらのうち
１種または２種以上を用いることができ、濃度としては
、５〜３０％が好ましい．反応に用いるラクトースとＮ
−アセチルグルコサミンの量は，モル比でｌ：１−１：
５とし、全基質濃度として２０〜７０％とするのが好ま
しい．また、本発明に用いるβ−ガラクトシダーゼは、
反応系において０． ５０／ｎ＋氾〜５０／ｍ Ｑとな
るように添加し、ＰＨ４〜９、温度５℃〜５０℃に保持
し，２時間〜５０時間作用させるのが好ましい。Detailed Description of the Invention (Industrial Application Field) The present invention relates to a method for producing N-acetyllactosamine contained in the sugar chains of large milk oligosaccharides and complex carbohydrates. (Prior art) ) N-acetyllactosamine is an amino disaccharide in which galactose and N-acetylglucosamine are linked with β-l.4, and was first isolated from the decomposition product of blood group glycoprotein. , is a biochemically very important oligosaccharide that exists in the sugar chains of various glycoproteins and glycolipids.It is also known as a growth factor for bifidobacteria, which is one of the intestinal muscle cells, and is highly functional. It is also a useful substance as a food material. Traditionally, N-acetyllactosamine has been manufactured by chemical synthesis or by combining the high-energy compound LIDP-galactose and N-acetyllactosamine.
It is known that lactose is synthesized using lactose synthetase using acetylglucosamine as a substrate, but these methods are complicated and expensive, and are still difficult to manufacture industrially. On the other hand, as a simple method, Lactobacillus bifidus (Lactobacillus bifidus) is grown using lactose and N-acetylglucosamine as substrates.
There have been reports using live bacterial cells of S. bifidusl and S. orobolomyces singularis [J. Bi-ol. chem. ．．
217.79 (1955). Can. J. Chem.
, 42, 2307 (19641) and a report on the action of β-galactosidase produced by Lactobacillus bifidus [J. Riot. Chem.
208, 299 (1954)]. or,
Recently, galactose and N-acetylglucosamine have been used as substrates for Escherichia coli.
A report on the production of N-acetyllactosamine through a dehydration condensation reaction using β-galactosidase produced by A. coli [Proceedings of the 10th Carbohydrate Symposium, p.i.
o7+tc+a7)] is shown. <Problems to be Solved by the Invention> However, both production methods have the drawback that the amount of N-acetyllactosamine produced is very small. Therefore, as a result of various studies in order to solve the above-mentioned drawbacks, the present inventors decided to use lactose and N-acetylglucosamine as substrates,
The present inventors have discovered that the amount of N-acetyllactosamine produced increases by allowing galactosidase to act in the presence of a salting-out agent, leading to the completion of the present invention. <Means for Solving the Problems> The present invention uses lactose and N-acetylglucosamine as substrates, allows β-galactosidase to act in the presence of a dissipating agent, and efficiently produces N-acetyllactosamine through a galactose transfer reaction. The purpose is to provide a method to do this. -acill as β-galactosidase used in the present invention
For example, enzymes originating from P. circulans can be used, and these commercially available enzymes can be used. Examples of the salting-out agent of the present invention include ammonium sulfate, sodium sulfate, potassium phosphate, magnesium sulfate, sodium citrate, and sodium chloride, and one or more of these can be used, and the concentration is: 5 to 30% is preferable. Lactose and N used in the reaction
-The amount of acetylglucosamine is in molar ratio l:1-1:
5, and the total substrate concentration is preferably 20 to 70%. Furthermore, the β-galactosidase used in the present invention is
0 in the reaction system. It is preferable to add it so that it becomes 50/n+flood to 50/mQ, maintain the pH at 4 to 9, the temperature at 5°C to 50°C, and let it act for 2 hours to 50 hours.
上記のようにして得られた反応液は、加熱により反応を
停止させ、生成したＮ−アセチルラクトサミンを必要に
応じて活性炭カラムクロマトグラフィー、ゲル濾過、高
速液体クロマトグラフィー等の手段を組み合わせて精製
することができる．
〈実施例〉
以下に、本発明の実、施例について、さらに具体的に説
明するが、かかる説明によって本発明が何ら限定されな
いことは勿論である．２０％硫酸アンモニウムを含む０
．１Ｍリン酸緩衝液（ｐＨ７．０１ にラクトース０．
９ｇとＮ−アセチルグルコサミンｌ．ｌｇ （モル比１
：２）を溶解した５１１Ｒの溶液に、市販β−ガラクト
シダーゼ（ケイアイ化成＠：ラクターゼＳ）を１２Ｕ添
加し、３０℃で３６時間反応させた．次に反応液は、５
分間の煮沸により反応を停止させ、Ｎ−アセチルラクト
サミンの生成量を高速液体クロマトグラフィーにより測
定した．本反応により、１１０ａ＋ｇのＮ−アセチルラ
クトサミンが製造された．
（比較例〉
本発明による実施例と同様の反応を硫酸アンモニウムを
含まない系で行い、Ｎ−アセチルラクトサミンの生成量
の変化を高速液体クロマトグラフィーにより測定し比較
した．その測定結果は図に示したとおりで、Ｎ−アセチ
ルラクトサミンの生成量が、約１．５倍になっているこ
とがわかる．
β−ガラクトシダーゼの酵素活性の測定１０ｍ ＭのＯ
ＮＰ−Ｇａｌ （才ルトーニトロフェニルガラクトシド
）溶液０．２ｍｆｆと０．１Ｍリン酸緩衝液（ｐＨ７
） ０．７ｇ＋．ｅを混合し、適当濃度に希釈した酵素
液０．１ｏｆｆを加え、３０゜Ｃで反応を行った．
ｌ Ｍ Ｎ ａｇｃ Ｏｓ２ｆｆＩ１２を加え、反応停
止後、才ルトーニトロフェノールの吸収である４２０ｎ
ｍの吸光度を測定した。酵素活性ＩＵは、１分間にｌｕ
ｎｏｌｅのオルトーニト口フェノールを遊離する酵素量
と定義した．Ｎ−アセチルラクトサミンの分析
実施例で得られた反応液は、次の高速液体クロマトグラ
フィーの条件で測定した．カラム： ＹＭＣ−Ｐａｃ
ｋ ＰＡ−０３ （４．６ ｘ ２５０ｍｓ＋１移動層
： アセトニトリル：水＝８０：２０流 速： ０．
８ｍｆｆ ／ ｎ＋ｉｎ．温 度：２５℃
検 出： Ｕ Ｖ ｍｌｌｌａｍ
試
料：
ｌＯμ
１The reaction solution obtained as described above is heated to stop the reaction, and the generated N-acetyllactosamine is purified by a combination of activated carbon column chromatography, gel filtration, high performance liquid chromatography, etc. as necessary. can do. <Examples> Examples of the present invention will be explained in more detail below, but it goes without saying that the present invention is not limited by such explanations. 0 containing 20% ammonium sulfate
．． 1M phosphate buffer (pH 7.01 with 0.0% lactose)
9g and N-acetylglucosamine l. lg (molar ratio 1
:2) was dissolved in 511R, 12 U of commercially available β-galactosidase (KAI Kasei @: Lactase S) was added, and the mixture was reacted at 30°C for 36 hours. Next, the reaction solution was
The reaction was stopped by boiling for a minute, and the amount of N-acetyllactosamine produced was measured by high performance liquid chromatography. Through this reaction, 110a+g of N-acetyllactosamine was produced. (Comparative example) The same reaction as in the example according to the present invention was carried out in a system not containing ammonium sulfate, and the change in the amount of N-acetyllactosamine produced was measured and compared using high performance liquid chromatography.The measurement results are shown in the figure. It can be seen that the amount of N-acetyllactosamine produced has increased approximately 1.5 times. Measurement of enzyme activity of β-galactosidase 10 mM O
0.2 mff of NP-Gal (nitrophenyl galactoside) solution and 0.1 M phosphate buffer (pH 7)
) 0.7g+. 0.1 off of the enzyme solution diluted to an appropriate concentration was added, and the reaction was carried out at 30°C.
l M N agc Os2ffI12 was added and after the reaction was stopped, 420n
The absorbance of m was measured. Enzyme activity IU is lu per minute
It was defined as the amount of enzyme that releases the ortho-nitrophenol of nole. The reaction solution obtained in the N-acetyllactosamine analysis example was measured under the following high performance liquid chromatography conditions. Column: YMC-Pac
k PA-03 (4.6 x 250ms+1 moving phase: acetonitrile:water = 80:20 flow rate: 0.
8mff/n+in. Temperature: 25℃ Detection: UV mllam Sample: 1Oμ 1
図面は本発明による塩析剤の添加効果を示したものであ
る．
特許The drawing shows the effect of adding the salting-out agent according to the present invention. patent
Claims (3)
し、β−ガラクトシダーゼを塩析剤存在下で作用させる
ことを特徴とするＮ−アセチルラクトサミンの製造方法
。(1) A method for producing N-acetyllactosamine, which comprises using lactose and N-acetylglucosamine as substrates and allowing β-galactosidase to act in the presence of a salting-out agent.
ン酸カリウム、硫酸マグネシウム、クエン酸ナトリウム
、塩化ナトリウムのうち、１種又は２種以上を用いる、
請求項１記載のＮ−アセチルラクトサミンの製造方法。(2) The salting-out agent uses one or more of ammonium sulfate, sodium sulfate, potassium phosphate, magnesium sulfate, sodium citrate, and sodium chloride,
The method for producing N-acetyllactosamine according to claim 1.
のＮ−アセチルラクトサミンの製造方法。(3) The method for producing N-acetyllactosamine according to claim 1, wherein the concentration of the salting-out agent is 5 to 30%.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP18491989A JP2819313B2 (en) | 1989-07-18 | 1989-07-18 | Method for producing N-acetyllactosamine |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP18491989A JP2819313B2 (en) | 1989-07-18 | 1989-07-18 | Method for producing N-acetyllactosamine |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH0349693A true JPH0349693A (en) | 1991-03-04 |
| JP2819313B2 JP2819313B2 (en) | 1998-10-30 |
Family
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP18491989A Expired - Fee Related JP2819313B2 (en) | 1989-07-18 | 1989-07-18 | Method for producing N-acetyllactosamine |
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| Country | Link |
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| JP (1) | JP2819313B2 (en) |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2001292791A (en) * | 2000-04-13 | 2001-10-23 | Seikagaku Kogyo Co Ltd | Method for producing n-acetyllactosmine |
| JP2006223268A (en) * | 2005-02-21 | 2006-08-31 | Yakult Honsha Co Ltd | Method for producing galactosyl disaccharides |
| US7883874B2 (en) | 2003-06-30 | 2011-02-08 | Clasado Inc. | Galactooligosaccharide composition and the preparation thereof |
| US8030049B2 (en) | 2006-01-31 | 2011-10-04 | Clasado Inc. | Galactosidase with α-galactosyltransferase activity |
| US8058047B2 (en) | 2005-12-20 | 2011-11-15 | Clasado, Inc. | α-galactosidase with transgalactosylating activity |
| US8168414B2 (en) | 2006-03-28 | 2012-05-01 | Clasado Inc. | Beta-galactosidase with transgalactosylating activity |
-
1989
- 1989-07-18 JP JP18491989A patent/JP2819313B2/en not_active Expired - Fee Related
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2001292791A (en) * | 2000-04-13 | 2001-10-23 | Seikagaku Kogyo Co Ltd | Method for producing n-acetyllactosmine |
| US7883874B2 (en) | 2003-06-30 | 2011-02-08 | Clasado Inc. | Galactooligosaccharide composition and the preparation thereof |
| JP2006223268A (en) * | 2005-02-21 | 2006-08-31 | Yakult Honsha Co Ltd | Method for producing galactosyl disaccharides |
| US8058047B2 (en) | 2005-12-20 | 2011-11-15 | Clasado, Inc. | α-galactosidase with transgalactosylating activity |
| US8030049B2 (en) | 2006-01-31 | 2011-10-04 | Clasado Inc. | Galactosidase with α-galactosyltransferase activity |
| US8168414B2 (en) | 2006-03-28 | 2012-05-01 | Clasado Inc. | Beta-galactosidase with transgalactosylating activity |
Also Published As
| Publication number | Publication date |
|---|---|
| JP2819313B2 (en) | 1998-10-30 |
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