Biochemistry

Using biochemical technology cultivated over many years, we extract and purify functional ingredients such as various enzymes, proteins, and nucleic acids from natural products such as animal tissues, and provide them to the pharmaceutical and food industries. We are also engaged in the development of industrial manufacturing methods for optically active compounds using microorganism-based capitalization methods and enzymatic optical resolution technologies. We also manufacture and sell sialic acid using recombinant enzymes.
In addition, we are also engaged in the research and development of new products in collaboration with universities and other research institutions and start-up companies.

Business and Technology
Product List

Bio-Based Optical Resolution Technology
Contributing to Drug Development with Proprietary Biotechnologies

In order to meet the increasing needs for optically active compounds in recent years, we are focusing on research and development of optically active compounds utilizing stereoselectivity of microorganisms and enzymes.
We are also developing production technologies for alcohols, carboxylic esters, and their derivatives with high optical purity using our proprietary biotechnologies such as capitalization and enzymatic methods.

Sialic Acid Business
The World’s Leading Supplier with Various Patents

Sialic acid, which exists at the ends of sugar chains on the cell surface, is a kind of acidic sugar that transmits information between cells and performs receptor-like functions. Naturally occurring sialic acid is found in the nests of sea swallows, milk, eggs, etc., but the amount of sialic acid produced from these sources is limited in terms of quantity and cost.
Sanyo Fine has succeeded in producing high quality sialic acid in large quantities at low cost using its proprietary technology. Today, sialic acid is attracting attention for its application in pharmaceuticals and reagents, such as for use in anti-influenza drugs.

Pharmacological Function	・Learning ability improvement effect ・Infection prevention effect ・Phlegm expectorant effect ・Therapeutic effect on amyotrophy	Applications	・Research reagent ・Raw materials for pharmaceuticals ・Raw materials for diagnostic reagents ・Virus filters ・Virus sensors

Pharmacological Function
・Learning ability improvement effect
・Infection prevention effect
・Phlegm expectorant effect
・Therapeutic effect on amyotrophy
Applications
・Research reagent
・Raw materials for pharmaceuticals
・Raw materials for diagnostic reagents
・Virus filters
・Virus sensors

Formula

Sialic Acid (N-Acetylneuraminic Acid: NeuAc)

Sialic acid has been applied to medicines effective against influenza viruses.

Influenza viruses bind to and then invade the cells of the target of infection. They proliferate within the cells, and then exit the cell to infect other cells. The virus is shaped like a “chestnut” with numerous spike-like protrusions. There are two types of protrusions, which act as a “glue” and “scissors,” respectively.
First, the virus utilizes the “glue” protrusions to attach to sialic acid on the cell surface. Then it infiltrates into the cell and proliferats. Next, by use of the “scissors” protrusions, the proliferated viruses exfiltrate from the cell by breaking the bonds between them and the cell. The exfiltrated viruses invade other cells one after another with the same propagation mechanism.
An anti-influenza drug, made from our sialic acid, relieves flu symptoms by neutralizing the function of these “scissors. This means that viruses that have entered cells and multiplied cannot leave the cells, even if they multiply, because the “scissors” are neutralized by the drug.

Carbohydrate Related Compounds
Nucleic acid relatives
Enzymes

Carbohydrate Related Compounds

N-Acetylneuraminic acid [NANA; Sialic acid; NeuAc] [CAS RN: 131-48-6]

Prepared by enzymatic synthesis from N-acetylglucosamine and pyruvic acid.^*1

References
- *1 I. Maru, J. Ohnishi, Y. Ohta and Y. Tsukada, Carbohydr. Res., 306, 575 (1998).

Formula

C₁₁H₁₉NO₉ (MW: 309.27)

CAS RN	131-48-6	Appearance	White crystalline powder
Purity	More than 99% (HPLC)	Package	1 g, 10 g, 100 g, 500 g, Bulk

CAS RN
131-48-6
Appearance
White crystalline powder
Purity
More than 99% (HPLC)
Package
1 g, 10 g, 100 g, 500 g, Bulk

N-Acetyl-D-mannosamine, monohydrate [ManNAc] [CAS RN: 7772-94-3]

N-Acetyl-D-mannosamine is an isomer of N-acetyl-D-glucosamine. It has attracted attention not only as an analytical standard but also for its use in the study of amino sugar metabolism and as an additive for animal cell culture. In recent years, there have been reports ^*1-*3 on the synthesis of sialic acid derivatives from derivatives of N-acetyl-D-mannosamine by condensation reaction with pyruvic acid using sialic acid aldolase.

References
- *1 M. J. Kim, W. J. Hennen, H. M. Sweers and C. H. Wong, J. Am. Chem. Soc., 110, 6481-6486 (1988).
- *2 C. Auge, B. Bouxom, B. Cavaye and C. Gautheron, Tetrahedron Lett., 30, 2217-2220 (1989).
- *3 C. C. Lin, C. H. Lin and C. H. Wong, Tetrahedron Lett., 38, 2649-2652 (1997).

Formula

C₈H₁₅NO₆・H₂O (MW:239.2)

CAS RN	7772-94-3	Appearance	White amorphous powder
Purity	More than 99% (HPLC)	Package	1 g, 10 g, Bulk

CAS RN
7772-94-3
Appearance
White amorphous powder.
Purity
More than 99% (HPLC)
Package
1 g, 10 g, Bulk

2,3-Dehydro-2-deoxy-N-acetylneuraminic acid [NeuAc2en; NeuNAc2en; Neu5Ac2en] [CAS RN: 24967-27-9]

Prepared by chemical synthesis from N-acetylneuraminic acid. Purified by column chromatography and crystalization.

Formula

C₁₁H₁₇NO₈ (MW: 291.25)

CAS RN	24967-27-9	Appearance	White crystalline powder
Purity	More than 95% (HPLC)	Package	25 mg, Bulk

CAS RN
24967-27-9
Appearance
White crystalline powder
Purity
More than 95% (HPLC)
Package
25 mg, Bulk

N-Acetylneuraminic acid oligomer, sodium salt

Prepared by hydrolysis of colominic acid.

Formula
n = 0 to 4
Dimer (DP2): C₂₂H₃₄N₂O₁₇Na₂ (MW: 644.5) Trimer (DP3): C₃₃H₅₀N₃O₂₅Na₃ (MW: 957.73) Tetramer (DP4): C₄₄H₆₆N₄O₃₃Na₄ (MW: 1270.97) Pentamer (DP5): C₅₅H₈₂N₅O₄₁Na₅ (MW: 1584.21) Hexamer (DP6): C₆₆H₉₈N₆O₄₉Na₆ (MW: 1897.45)

CAS RN		Appearance	White lyophilized powder
Purity	More than 95% (HPLC)	Package	DP2: 100 mg DP3 to DP6: 25 mg each

CAS RN
Appearance
White lyophilized powder
Purity
More than 95% (HPLC)
Package
DP2: 100 mg
DP3 to DP6: 25 mg each

Cytidine-5′-monophospho-N-acetylneuraminic acid, disodium salt [CMP-Neu5Ac·2Na] [CAS RN: 3063-71-6]

Prepared by enzymatic synthesis from N-acetylneuraminic acid and CTP. Purified by ion-exchange column chromatography and lyophilization.

Formula

C₂₀H₂₉N₄O₁₆PNa₂ (MW: 658)

CAS RN	3063-71-6	Appearance	White lyophilized powder
Purity	More than 95% (HPLC) (Water content: 10% or less)	Package	10 mg, 100 mg, 1 g, Bulk

CAS RN
3063-71-6
Appearance
White lyophilized powder
Purity
More than 95% (HPLC) (Water content: 10% or less)
Package
10 mg, 100 mg, 1 g, Bulk

Uridine-5′-diphosphoglucose, disodium salt [CAS RN: 28053-08-9]

Formula

C₁₅H₂₂N₂O₁₇P₂Na₂ (MW: 610.3)

CAS RN	28053-08-9	Appearance	White crystalline powder
Purity	More than 98% (Water content: approx. 7%)	Package	1 g

CAS RN
28053-08-9
Appearance
White crystalline powder
Purity
More than 98% (Water content: approx. 7%)
Package
1 g

Uridine-5′-diphosphoglucuronic acid, trisodium salt [CAS RN: 63700-19-6]

This product can be used as a substrate for glucuronidation for the purpose of pharmacokinetic studies.

Formula

C₁₅H₁₉N₂O₁₈P₂Na₃ (MW: 646.3)

CAS RN	63700-19-6	Appearance	White crystalline powder
Purity	More than 98% (Water content: 12% or less)	Package	10 g, Bulk

CAS RN
63700-19-6
Appearance
White crystalline powder
Purity
More than 98% (Water content: 12% or less)
Package
10 g, Bulk

Nucleic acid relatives

Deoxyribonucleotides (monophosphates, triphosphates)

Enzymes

We extract and purify enzymes and other functional ingredients from natural products such as animal tissues, using large freeze-drying equipment and other facilities.

N-Acetylneuraminic acid aldolase; N-Acetylneuraminic pyruvate lyase [ EC 4.1.3.3 ]

Origin	Escherichia coli	Reaction	N-Acetylneuraminate → N-Acetyl-D-mannosamine + pyruvate
Appearance	White amorphous powder	Package	10 units, Bulk

Origin
Escherichia coli
Reaction
N-Acetylneuraminate → N-Acetyl-D-mannosamine + pyruvate
Appearance
White amorphous powder
Package
10 units, Bulk

Properties

Molecular weight	Approx. 98,000 Da (gel filtration)
Substrate specificity	N-glycolylneuraminic acid (NGNA) is cleaved as well as NANA.

Molecular weight
Approx. 98,000 Da (gel filtration)
Substrate specificity
N-glycolylneuraminic acid (NGNA) is cleaved as well as NANA.

Neuraminidase [Sialidase]; Acylneuraminyl Hydrolase [ EC 3.2.1.18 ]

Origin	Arthrobacter ureafaciens	Reaction	Sialyl compound → Sialic acid ＋ Asialocompound
Appearance	White lyophilized powder	Package	5 units, 100 units, Bulk

Origin
Arthrobacter ureafaciens
Reaction
Sialyl compound → Sialic acid ＋ Asialocompound
Appearance
White lyophilized powder
Package
5 units, 100 units, Bulk

Properties

This enzyme consist of four isozymes (L, M1, M2, S).

Molecular weight	Approx. 52,000 Da, 66,000 Da and 88,000 Da (gel filtration, SDS-PAGE)
Substrate specificity	The α-ketosidic linkage of N-glycolylneuraminic acid (NGNA) can be hydrolyzed as well as that of NANA. This enzyme cleaves α(2→3), α(2→6) and α(2→8) linkages of N-acetylneuraminic acid in glycoconjugates. The acivity is independent on Ca²⁺ and is not inhibited by EDTA, which is in striking contrast to Vibrio cholerae neuraminidase, and is not or slightly inhibited by inhibitors such as monoiodoacetate, p-chloromercuribenzoate and HgCl₂, which is in striking contrast to Clostridium perfringens neuraminidase.

Molecular weight
Approx. 52,000 Da, 66,000 Da and 88,000 Da (gel filtration, SDS-PAGE)
Substrate specificity
The α-ketosidic linkage of N-glycolylneuraminic acid (NGNA) can be hydrolyzed as well as that of NANA. This enzyme cleaves α(2→3), α(2→6) and α(2→8) linkages of N-acetylneuraminic acid in glycoconjugates. The acivity is independent on Ca²⁺ and is not inhibited by EDTA, which is in striking contrast to Vibrio cholerae neuraminidase, and is not or slightly inhibited by inhibitors such as monoiodoacetate, p-chloromercuribenzoate and HgCl₂, which is in striking contrast to Clostridium perfringens neuraminidase.

Neuraminidase isozyme S [Reagent for studies of gangliosides]

Origin	Arthrobacter ureafaciens
Appearance	White amorphous powder	Package	1 unit, 5 units

Origin
Arthrobacter ureafaciens
Appearance
White amorphous powder
Package
1 unit, 5 units

Properties

Molecular weight	Approx. 52,000 Da (gel filtration, SDS-PAGE)
Substrate specificity	sozyme S cleaves α(2→3), α(2→6) and α(2→8) linkages of N-acetylneuraminic acid in glycoconjugates. In the absence of detergents and calcium ion, the enzyme hydrolyzes N-acetylneuraminosyl moiety of polysialogangliosides and produces monosialoganglioside GM1, while in the presence of detergents (Na-cholate, Triton X-100 etc.), GM1 is further desialylated to asialoganglioside GA1. the character of the enzyme is similar to Vibrio cholerae neuraminidase except requirement of Ca²⁺ in the latter.

Molecular weight
Approx. 52,000 Da (gel filtration, SDS-PAGE)
Substrate specificity
sozyme S cleaves α(2→3), α(2→6) and α(2→8) linkages of N-acetylneuraminic acid in glycoconjugates. In the absence of detergents and calcium ion, the enzyme hydrolyzes N-acetylneuraminosyl moiety of polysialogangliosides and produces monosialoganglioside GM1, while in the presence of detergents (Na-cholate, Triton X-100 etc.), GM1 is further desialylated to asialoganglioside GA1. the character of the enzyme is similar to Vibrio cholerae neuraminidase except requirement of Ca²⁺ in the latter.

3α-Hydroxysteroid dehydrogenase; 3α-Hydroxysteroid:NAD(P)+ oxidoreductase [ EC 1.1.1.50 ]

3α-Hydroxysteroid ⇄ 3-oxosteroid

Origin	Pseudomonas testosteroni
Appearance	White lyophilized powder	Package	Bulk

Origin
Pseudomonas testosteroni
Appearance
White lyophilized powder
Package
Bulk

Properties

Molecular weight	Approx. 37,000 Da

Molecular weight
Approx. 37,000 Da

β-Hydroxysteroid dehydrogenase; 3(or 17)β-Hydroxysteroid:NAD(P)+ oxidoreductase [ EC 1.1.1.51 ]

epi-androsterone ⇄ 5α-androstene-3,17-dione

testosterone ⇄ 4-androstene-3,17-dione

Origin	Pseudomonas testosteroni
Appearance	White amorphous powder	Package	10 units

Origin
Pseudomonas testosteroni
Appearance
White amorphous powder
Package
10 units

Properties

Molecular weight	Approx. 80,000 Da

Molecular weight
Approx. 80,000 Da

NADH oxidase [ EC 1.6.3.1 ]

Origin	Bacillus licheniformis	Reaction	NADH + H⁺ + O₂ → NAD⁺ + H₂O₂
Appearance	White lyophilized powder	Package	100 units, Bulk

Origin
Bacillus licheniformis
Reaction
NADH + H⁺ + O₂ → NAD⁺ + H₂O₂
Appearance
White lyophilized powder
Package
100 units, Bulk

Properties

Molecular weight	Approx. 240,000 Da
Substrate specificity	In the absence of added FAD both NADH and NADPH are oxidized equally, but by the addition of FAD (about 30 μM) to reaction mixture the reaction velocity to NADH is accelerated about 20–30 times in contrast to 2–3 times of NADPH. Accordingly, the substrate specificity of NADH is about 10 times larger than that of NADPH in the presence of added FAD.

Molecular weight
Approx. 240,000 Da
Substrate specificity
In the absence of added FAD both NADH and NADPH are oxidized equally, but by the addition of FAD (about 30 μM) to reaction mixture the reaction velocity to NADH is accelerated about 20–30 times in contrast to 2–3 times of NADPH. Accordingly, the substrate specificity of NADH is about 10 times larger than that of NADPH in the presence of added FAD.

Elastase [ EC 3.4.21.36 ]

Enzymatic API for improving lipid metabolism disorders.
Prepared by use of large freeze-drying equipment and other facilities.

Kalliginogenase [ EC 3.4.21.35 ]

Enzymatic API for improving circulatory disorders.
Prepared by use of large freeze-drying equipment and other facilities.

Phospholipase A2 [ EC 3.1.1.4 ]

For better quality of food with our original technology of extraction and purification

Phospholipase A2 is distributed widely in living organisms and well-known to digest phospholipids from plants and produce bioactive substances such as prostaglandine by a hydrolysis of phospholipids in the cell membrane. SANYO FINE has original technologies for extraction and purification of phospholipase A2 from swine pancreas. Lysonase is one of our products containing phspholipase A2 with high potency and its ability is stereo-selective hydrolysis of the ester at 2-position of glycero-phospholipids. We can supply them both as aqueous solution and powder form depending on our customer’s need.

Phospholipase A2 converts lecithin, which is contained in egg yolk and soybean, to lysolecithin by a hydrolysis. Lysolecithin has much ability of emulsification than that of lecithin and is used as emulsion stabilizer for ice-cream and mayonnaise, dispersion stabilizer for chocolate and quality improvement for dough.

Biochemistry

Bio-Based Optical Resolution Technology

Contributing to Drug Development with Proprietary Biotechnologies

Sialic Acid Business

The World’s Leading Supplier with Various Patents

Sialic acid has been applied to medicines effective against influenza viruses.

Carbohydrate Related Compounds

N-Acetylneuraminic acid [NANA; Sialic acid; NeuAc] [CAS RN: 131-48-6]

N-Acetyl-D-mannosamine, monohydrate [ManNAc] [CAS RN: 7772-94-3]

2,3-Dehydro-2-deoxy-N-acetylneuraminic acid [NeuAc2en; NeuNAc2en; Neu5Ac2en] [CAS RN: 24967-27-9]

N-Acetylneuraminic acid oligomer, sodium salt

Cytidine-5′-monophospho-N-acetylneuraminic acid, disodium salt [CMP-Neu5Ac·2Na] [CAS RN: 3063-71-6]

Uridine-5′-diphosphoglucose, disodium salt [CAS RN: 28053-08-9]

Uridine-5′-diphosphoglucuronic acid, trisodium salt [CAS RN: 63700-19-6]

Nucleic acid relatives

Enzymes

N-Acetylneuraminic acid aldolase; N-Acetylneuraminic pyruvate lyase [ EC 4.1.3.3 ]

Properties

Neuraminidase [Sialidase]; Acylneuraminyl Hydrolase [ EC 3.2.1.18 ]

Properties

Neuraminidase isozyme S [Reagent for studies of gangliosides]

Properties

3α-Hydroxysteroid dehydrogenase; 3α-Hydroxysteroid:NAD(P)+ oxidoreductase [ EC 1.1.1.50 ]

Properties

β-Hydroxysteroid dehydrogenase; 3(or 17)β-Hydroxysteroid:NAD(P)+ oxidoreductase [ EC 1.1.1.51 ]

Properties

NADH oxidase [ EC 1.6.3.1 ]

Properties

Elastase [ EC 3.4.21.36 ]

Kalliginogenase [ EC 3.4.21.35 ]

Phospholipase A2 [ EC 3.1.1.4 ]

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