Abstract
β-Mannanase (endo-l,4-β-mannanase; mannan endo-1,4-β-mannosidase; EC 3.2.1.78) catalyzes endo-wise hydrolysis of the backbone of mannan and heteromannans, including hemicellulose polysaccharides, which are among the major components of plant cell walls. The gene manl, which encodes β- mannanase, of the filamentous fungus Trichoderma reesei was isolated from an expression library by using antiserum raised towards the earlier-purified β- mannanase protein. The deduced β-mannanase consists of 410 amino acids. On the basis of hydrophobic cluster analysis, the β-mannanase was assigned to family 5 of glycosyl hydrolases (cellulase family A). The C terminus of the β-mannanase has strong amino acid sequence similarity to the cellulose binding domains of fungal cellulases and is preceded by a serine-, threonine- , and proline-rich region. Consequently, the β-mannanase is probably organized similarly to the T. reesei cellulases, having a catalytic core domain separated from the substrate-binding domain by an O-glycosylated linker. Active β-mannanase was expressed and secreted by using the yeast Saccharomyces cerevisiae as the host. The results indicate that the manl gene encodes the two β-mannanases with different isoelectric points (pIs 4.6 and 5.4) purified earlier from T. reesei.
| Original language | English |
|---|---|
| Pages (from-to) | 1090-1097 |
| Number of pages | 8 |
| Journal | Applied and Environmental Microbiology |
| Volume | 61 |
| Issue number | 3 |
| Publication status | Published - 1 Jan 1995 |
| MoE publication type | A1 Journal article-refereed |
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Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei β-mannanase gene containing a cellulose binding domain. / Stalbrand, H.; Saloheimo, A.; Vehmaanpera, J.; Henrissat, B.; Penttila, M.
In: Applied and Environmental Microbiology, Vol. 61, No. 3, 01.01.1995, p. 1090-1097.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei β-mannanase gene containing a cellulose binding domain
AU - Stalbrand, H.
AU - Saloheimo, A.
AU - Vehmaanpera, J.
AU - Henrissat, B.
AU - Penttila, M.
PY - 1995/1/1
Y1 - 1995/1/1
N2 - β-Mannanase (endo-l,4-β-mannanase; mannan endo-1,4-β-mannosidase; EC 3.2.1.78) catalyzes endo-wise hydrolysis of the backbone of mannan and heteromannans, including hemicellulose polysaccharides, which are among the major components of plant cell walls. The gene manl, which encodes β- mannanase, of the filamentous fungus Trichoderma reesei was isolated from an expression library by using antiserum raised towards the earlier-purified β- mannanase protein. The deduced β-mannanase consists of 410 amino acids. On the basis of hydrophobic cluster analysis, the β-mannanase was assigned to family 5 of glycosyl hydrolases (cellulase family A). The C terminus of the β-mannanase has strong amino acid sequence similarity to the cellulose binding domains of fungal cellulases and is preceded by a serine-, threonine- , and proline-rich region. Consequently, the β-mannanase is probably organized similarly to the T. reesei cellulases, having a catalytic core domain separated from the substrate-binding domain by an O-glycosylated linker. Active β-mannanase was expressed and secreted by using the yeast Saccharomyces cerevisiae as the host. The results indicate that the manl gene encodes the two β-mannanases with different isoelectric points (pIs 4.6 and 5.4) purified earlier from T. reesei.
AB - β-Mannanase (endo-l,4-β-mannanase; mannan endo-1,4-β-mannosidase; EC 3.2.1.78) catalyzes endo-wise hydrolysis of the backbone of mannan and heteromannans, including hemicellulose polysaccharides, which are among the major components of plant cell walls. The gene manl, which encodes β- mannanase, of the filamentous fungus Trichoderma reesei was isolated from an expression library by using antiserum raised towards the earlier-purified β- mannanase protein. The deduced β-mannanase consists of 410 amino acids. On the basis of hydrophobic cluster analysis, the β-mannanase was assigned to family 5 of glycosyl hydrolases (cellulase family A). The C terminus of the β-mannanase has strong amino acid sequence similarity to the cellulose binding domains of fungal cellulases and is preceded by a serine-, threonine- , and proline-rich region. Consequently, the β-mannanase is probably organized similarly to the T. reesei cellulases, having a catalytic core domain separated from the substrate-binding domain by an O-glycosylated linker. Active β-mannanase was expressed and secreted by using the yeast Saccharomyces cerevisiae as the host. The results indicate that the manl gene encodes the two β-mannanases with different isoelectric points (pIs 4.6 and 5.4) purified earlier from T. reesei.
UR - http://www.scopus.com/inward/record.url?scp=0028932041&partnerID=8YFLogxK
M3 - Article
C2 - 7793911
AN - SCOPUS:0028932041
VL - 61
SP - 1090
EP - 1097
JO - Applied and Environmental Microbiology
JF - Applied and Environmental Microbiology
SN - 0099-2240
IS - 3
ER -