Purification and characterization of five cellulases and one xylanase from Penicillium brasilianum IBT 20888
(2003) In Enzyme and Microbial Technology 32(7). p.851-861- Abstract
- The filamentous fungus Penicillium brasilianum IBT 20888 was cultivated on a mixture of 30 g l−1 cellulose and 10 g l−1 xylan for 111 h and the resulting culture filtrate was used for protein purification. From the cultivation broth, five cellulases and one xylanase were purified. Hydrolysis studies revealed that two of the cellulases were acting as cellobiohydrolases by being active on only microcrystalline cellulose (Avicel). Three of the cellulases were active on both Avicel and carboxymethyl cellulose indicating endoglucanase activity. Two of these showed furthermore mannanase activity by being able to hydrolyze galactomannan (locust bean gum). Adsorption studies revealed that the smaller of the two enzymes was not able to bind to... (More)
- The filamentous fungus Penicillium brasilianum IBT 20888 was cultivated on a mixture of 30 g l−1 cellulose and 10 g l−1 xylan for 111 h and the resulting culture filtrate was used for protein purification. From the cultivation broth, five cellulases and one xylanase were purified. Hydrolysis studies revealed that two of the cellulases were acting as cellobiohydrolases by being active on only microcrystalline cellulose (Avicel). Three of the cellulases were active on both Avicel and carboxymethyl cellulose indicating endoglucanase activity. Two of these showed furthermore mannanase activity by being able to hydrolyze galactomannan (locust bean gum). Adsorption studies revealed that the smaller of the two enzymes was not able to bind to cellulose. Similarity in molecular mass, pI and hydrolytic properties suggested that these two enzymes were identical, but the smaller one was lacking the cellulose-binding domain or an essential part of it. The basic xylanase (pI>9) was only active towards xylan. Two of the purified cellulases with endoglucanase activity were partly sequenced and based on sequence homology with known enzymes they were classified as belonging to families 5 and 12 of the glycosyl hydrolases. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/124652
- author
- Jørgensen, Henning ; Eriksson, Torny LU ; Börjesson, Johan LU ; Tjerneld, Folke LU and Olsson, Lisbeth
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Glycosyl hydrolase families 5 and 12, Mannanase, Endoglucanase, Cellobiohydrolase, Cellulose-binding domain, Adsorption
- in
- Enzyme and Microbial Technology
- volume
- 32
- issue
- 7
- pages
- 851 - 861
- publisher
- Elsevier
- external identifiers
-
- wos:000183345200011
- scopus:0038058833
- ISSN
- 0141-0229
- DOI
- 10.1016/S0141-0229(03)00056-5
- language
- English
- LU publication?
- yes
- id
- d17a7da8-e4cb-4242-b04a-4c5f14931730 (old id 124652)
- date added to LUP
- 2016-04-01 12:12:57
- date last changed
- 2022-04-29 02:12:32
@article{d17a7da8-e4cb-4242-b04a-4c5f14931730,
abstract = {{The filamentous fungus Penicillium brasilianum IBT 20888 was cultivated on a mixture of 30 g l−1 cellulose and 10 g l−1 xylan for 111 h and the resulting culture filtrate was used for protein purification. From the cultivation broth, five cellulases and one xylanase were purified. Hydrolysis studies revealed that two of the cellulases were acting as cellobiohydrolases by being active on only microcrystalline cellulose (Avicel). Three of the cellulases were active on both Avicel and carboxymethyl cellulose indicating endoglucanase activity. Two of these showed furthermore mannanase activity by being able to hydrolyze galactomannan (locust bean gum). Adsorption studies revealed that the smaller of the two enzymes was not able to bind to cellulose. Similarity in molecular mass, pI and hydrolytic properties suggested that these two enzymes were identical, but the smaller one was lacking the cellulose-binding domain or an essential part of it. The basic xylanase (pI>9) was only active towards xylan. Two of the purified cellulases with endoglucanase activity were partly sequenced and based on sequence homology with known enzymes they were classified as belonging to families 5 and 12 of the glycosyl hydrolases.}},
author = {{Jørgensen, Henning and Eriksson, Torny and Börjesson, Johan and Tjerneld, Folke and Olsson, Lisbeth}},
issn = {{0141-0229}},
keywords = {{Glycosyl hydrolase families 5 and 12; Mannanase; Endoglucanase; Cellobiohydrolase; Cellulose-binding domain; Adsorption}},
language = {{eng}},
number = {{7}},
pages = {{851--861}},
publisher = {{Elsevier}},
series = {{Enzyme and Microbial Technology}},
title = {{Purification and characterization of five cellulases and one xylanase from Penicillium brasilianum IBT 20888}},
url = {{http://dx.doi.org/10.1016/S0141-0229(03)00056-5}},
doi = {{10.1016/S0141-0229(03)00056-5}},
volume = {{32}},
year = {{2003}},
}