Skip to main content
. 2004 Aug;70(8):4522–4531. doi: 10.1128/AEM.70.8.4522-4531.2004

TABLE 4.

Comparison of properties of purified chitosanases produced by microorganismse

Microorganism Mol mass (kDa)a Action modef Optimum pH Sp. act (U/mg) Substrate specificity (% DDA)b Inducibilityc End productsd Source or reference
Bacillus sp. strain KCTC 0377BP 45 Endo 4.0-6.0 1,700 Chitosan (40-100), CMC (2.5) C G3-G7 This study
Aspergillus oryzae IAM2660 40 Endo 5.5 17.2 Chitosan (70-100) C Oligomer 51
135 Exo 5.5 38.8 Chitosan (90-100) I G1
Nocardia orientalis IFO 12806 97 Exo 5.5 35.8 Chitosan (100) I G1 28
Acinetobacter sp. strain CHB101 37 Endo 5-9 334 Chitosan (70-90) C G2, G3 39
30 Endo 5-9 800 Glycol chitosan C
Enterobacter sp. strain G-1 50 Exo 7.0 5.84 Chitosan (80) I G2 49
Myxobacter strain AL-1 31 Endo 5.0, 6.8 ND CMC, chitosan ND ND 32
Matsuebacter chitosanotabidus 3001 34 Endo 4.0 250 Chitosan (90) I G1-G3 31
B. cereus S1 45 Endo 6.0 196 Chitosan (ND), CMC (21.6) C G2-G4 20
B. megaterium P1 chitosanase A 43 Endo 4.5-6.5 154.8 Chitosan (81), CMC (0.4) I Oligomer 33
Bacillus sp. strain KFB-C108 48 Endo 6.5 110 Chitosan (ND) I G3-G5 50
a

Determined by SDS-PAGE analysis with purified enzyme.

b

Substrate specificity for chitosan and CMC. Data in parentheses indicate appropriate DDA of chitosan for the activity (more than 50% relative activity) and relative activity of CMC for chitosan.

c

C and I are abbreviations for constitutive and inducible, respectively.

d

End product of the enzymes using chitosan as the substrate.

e

ND, not determined.

f

Exo, exocleavage type; endo, endocleavage type.