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Enzyme Explorer

Carbohydrate Analysis

Complex Carbohydrates
Enzyme Index
  Alginate Lyase
Carbohydrate Index
  Alginic Acid
  Chondroitin Sulfates
  Heparan Sulfate
  Hyaluronic Acid
Kits and Reagents for Glycoprotein Analysis

Glycoprotein Analysis Manual

Hemicellulase, Xylanase, Hemicellulose and Xylan

Hemicellulose and Xylans
Hemicelluloses are a group of plant-derived heteropolysaccharides associated with cellulose and lignin. The most common hemicelluloses are: xylan, glucuronoxylan, arabinoxylan, glucomannan and xyloglucan. In angiosperms, the principal hemicellulose component, xylan, is a polymer of β(1-4)D-xylopyranose. In arabinoxylan, branching occurs at the C2 & C3 positions with α-L-arabinofunaose. Glucuronoxylan, also found in angiosperms, has the xylan backbone with 4-0 methylglucuronic acid branching. In addition, arabinose branching as well as acetylation may be present. Gymnosperms contain glucomannans comprised primarily of D-mannosyl and D-glucosyl residues.

from Aspergillus niger
Product Number H2125

An < mixture of glycolytic enzymes usually containing xylanase, mananase and other activities.

Synonyms: endo-1,4-β-xylanase

Xylanase catalyzes the endohydrolysis of 1,4-β-D-xylosidic linkages in xylans yielding various 1,4-β-D-xylooligosaccharides.

from Aureobasidium pullulans
Product Number X4001 (Lyophilized, 50-200 un/mg)

from Thermomyces lanuginosus
Product Number X2753 (Novozymes Pentopan Mono BG)

from Trichoderma virde
Product Number X3876 (Lyophilized, 100-300 un/mg)

1. Enzyme Nomenclature, (

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Chitinase and Chitin

Synonyms: 1,4-β-poly-N-acetylglucosaminidase

Chitinases are enzymes that catalyze the degradation of chitin. They have been detected in many organisms, including bacteria, fungi, plants, invertebrates and vertebrates.1,2 Chitinases are broadly classified as endo- and exochitinases. The endochitinase activity is defined as the random cleavage at internal points in the chitin chain. The exochitinase activity is defined as the progressive action starting at the non-reducing end of chitin with the release of chitobiose or N-acetylglucosamine units.2,3 Chitobiosidase and N-acetyl-b-glucosaminidase are considered exochitinases.2 The combination of endo- and exochitinases results in a synergistic increase in the chitinolytic activity.4

from Serratia marcescens
Product Number C1603 (400-1,200 un/g)
Product Number C1650 (min 10 un/g)

from Streptomyces griseus
Product Number C6137 (200-600 un/g)

from Trichoderma viride
Product Number C8241 minimum 200-600 un/g

1. Rogalski, J., et al., Acta Microbiol. Pol., 46, 363-375 (1997).
2. Tronsmo, A., and Harman, G.E., Anal. Biochem., 208, 74-79 (1993).
3. Felse, P.A., and Panda, T., Bioproc. Eng., 23, 127-134 (2000).
4. Bolar, J.P., et al., Transgenic Res., 10, 533-543 (2001).

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Chitosanase and Chitosan

Synonyms: chitosan N-acetylglucosaminohydrolase

Chitosanase catalyzes the endohydrolysis of β-1,4-linkages between D-glucosamine (GlcN-GlcN) residues in chitosan. The enzyme from Streptomyces has been reported to also hydrolyze the GlcNAc-GlcN linkage in partially acetylated chitosan.

from Streptomyces species
Product Number C0794 (glycerol solution, min 15 un/mg)

from Streptomyces griseus
Product Number C9830 (lyophilized, >50 un/mg)

2. Enzyme Nomenclature (
3. Fukamizo, T., et al., Reaction mechanism of chitosanase from Streptomyces sp. N174,. Biochem. J., 311, 377-83 (1995)

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Chondroitin and Chondroitinases

Chondroitinase ABC
(Formerly EC#
Synonyms: Chondroitin ABC Lyase

Chondroitinase ABC catalyzes the eliminative degradation of polysaccharides containing 1,4-β-D-hexosaminyl and 1,3-β-D-glucuronosyl or 1,3-α-L-iduronosyl linkages to disaccharides containing 4-deoxy-b-D-gluc-4-enuronosyl groups. It acts on chondroitin 4-sulfate, chondroitin 6-sulfate, dermatan sulfate, and acts slowly on hyaluronate.1 Initial rates of degradation of chondroitin sulfate B, chondroitin, and hyaluronic acid were 40%, 20%, and 2%, respectively, that of chondroitin sulfate A and chondroitin sulfate C.2

from Proteus vulgaris
Product Number C3667

4. Enzyme Nomenclature, p. 425, 1992 Academic Press, San Diego, California
5. Yamagata, T., et al., J. Biol. Chem., 243, 1523-1535 (1968).
6. Martinez, J.B., et al., J. Biol. Chem., 234, 2236 (1959).
7. Saito, H., et al., J. Biol. Chem., 243, 1536-1542 (1968).
8. Suzuki, S., et al., J. Biol. Chem., 243, 1543 (1968).
9. Oike, Y., et al., J. Biol. Chem., 257, 9751 (1982).

Chondroitinase AC
Synonym: Chondroitin AC Lyase

Chondroitinase AC is an eliminase that degrades chondroitin sulfates A and C, but not chondroitin sulfate B. The enzyme cleaves, via an elimination mechanism, sulfated and non-sulfated polysaccharide chains containing (1-4) linkages between hexosamines and glucuronic acid residues. The reaction yields oligosaccharide products, mainly disaccharides, containing unsaturated uronic acids that can be detected by UV spectroscopy at 232 nm.

The enzyme shows approximately equal activity with chondroitin sulfates A and C, while the activity observed with chondroitin sulfate B is approximately 7% of this value. This activity is most likely due to the presence of chondroitin sulfates A and C (10%) in the chondroitin sulfate B.

from Flavobacterium heparinum
Product Number C2780
Product Number E2039

1. Yamagata, T., et al., J. Biol. Chem., 243, 1523-1535 (1968).
2. Hiyama, K., and Okada, S., J. Biol. Chem., 250, 1824 (1975).
3. Tkalec, A.L., et al., Appl. Environ. Microbiol., 66, 29-35 (2000).

Chondroitinase C
EC# 4.2.2.-

Chondroitinase C cleaves chondroitin sulfate C producing tetrasaccharide plus an unsaturated 6-sulfated disaccharide (delta Di-6S). It also cleaves hyaluronic acid producing unsaturated nonsulfated disaccharide (delta Di-OS). Chondroitin sulfate A is also degraded producing oligosaccharides and delta Di-6S but not delta Di-4S.1 Chondroitinase C cleaves the GalNAc bond of the pentasaccharides or hexasaccharides derived from the linkage region of chondroitin sulfate chains and tolerated sulfation of the C-4 or C-6 of the GalNAc residue and C-6 of the Gal residues, as well as 2-O-phosphorylation of the Xyl residue. In contrast, it does not act on a GalNAc–GlcA linkage when attached to a 4-O-sulfated Gal residue.2

from Flavobacterium heparinum
Product Number C0954

1. Michelacci, Y.M., and Dietrich, C.,P., J. Biol. Chem., 251, 1154-8 (1976)
2. Tsuda, H., et al., Eur. J. Biochem. 262, 127-133 (1999)

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Dextranase and Dextrans

It is composed of approximately 95% α-D-(1-6) linkages. The remaining α(1-3) linkages account for the branching of dextran.1,2,3 Conflicting data on the branch lengths implies that the average branch length is less than three glucose units.4,5 However, other methods indicate branches of greater than 50 glucose units exist.6,7 Native dextran has been found to have a molecular weight (MW) in the range of 9 million to 500 million.8,9,10 Lower MW dextrans will exhibit slightly less branching4 and have a more narrow range of MW distribution.11 Dextrans with MW greater than 10,000 behave as if they are highly branched. As the MW increases, dextran molecules attain greater symmetry.7,12,13 Dextrans with MW of 2,000 to 10,000 dextran molecules exhibit the properties of an expandable coil.12 At MWs below 2,000 dextran is more rod-like.14

Synonym: 1,6-α-D-glucan 6-glucanohydrolase
Dextranase catalyzes the endohydrolysis of 1,6-α-D-glucosidic linkages in dextran. 15

from Penicillium species
Product Number D8144 (Lyophilized, 400-800 un/mg)
Product Number D5884 (Lyophilized, 100-200 un/mg)
Product Number D4668 (Lyophilized, 10-25 un/mg)
Product Number D0443 Novozymes Dextranase Plus L

1. Rankin, J.C. and Jeanes, A., J. Am. Chem. Soc., 76, 4435 (1954).
2. Dimler, R.J. et al., J. Am. Chem. Soc., 77, 6568 (1955).
3. Van Cleve, J.W. et al., J. Am. Chem. Soc., 78, 4435 (1956).
4. Lindberg, B. and Svensson, S., Acta. Chem. Scand., 22, 1907 (1968).
5. Larm, O. et al., Carbohydr. Res. 20, 39 (1971).
6. Bovey, F.A., J. Polym. Sci., 35, 167 (1959).
7. Senti, R.F. et al., J. Polym. Sci., 17, 527 (1955).
8. Arond, L.H. and Frank, H.P., J. Phys. Chem., 58, 953 (1954).
9. Elias, H.G., Makromol. Chem., 33, 166 (1959).
10. Antonini, E. et al., Biopolymers, 2, 27 (1964).
11. Supplier's data.
12. Granath, K.A., J. Colloid Sci., 13, 308 (1958).
13. Wales, M. at al., J. Polym. Sci., 66, 101 (1979).
14. Gekko, K., Am. Chem. Soc. Symposium Series, 150, 415 (1981).
15. Enzyme Nomenclature (

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