Role of the bga1-encoded extracellular β-galactosidase of Hypocrea jecorina in cellulase induction by lactose

Bernhard Seiboth, Lukas Hartl, Noora Salovuori, Karin Lanthaler, Geoff D. Robson, Jari Vehmaanperä, Merja E. Penttilä, Christian P. Kubicek

Research output: Contribution to journalArticleScientificpeer-review

60 Citations (Scopus)

Abstract

Lactose is the only soluble and economically feasible carbon source for the production of cellulases or heterologous proteins regulated by cellulase expression signals by Hypocrea jecorina (Trichoderma reesei). We investigated the role of the major β-galactosidase of H. jecorina in lactose metabolism and cellulase induction. A genomic copy of the bga1 gene was cloned, and this copy encodes a 1,023-amino-acid protein with a 20-amino-acid signal sequence. This protein has a molecular mass of 109.3 kDa, belongs to glycosyl hydrolase family 35, and is the major extracellular β-galactosidase during growth on lactose. Its transcript was abundant during growth on L-arabinose and L-arabinitol but was much less common when the organism was grown on lactose, D-galactose, galactitol, D-xylose, and xylitol. Δbga1 strains grow more slowly and accumulate less biomass on lactose, but the cellobiohydrolase I and II gene expression and the final cellulase yields were comparable to those of the parental strain. Overexpression of bga1 under the control of the pyruvate kinase promoter reduced the lag phase, increased growth on lactose, and limited transcription of cellobiohydrolases. We detected an additional extracellular β-galactosidase activity that was not encoded by bga1 but no intracellular β-galactosidase activity. In conclusion, cellulase production on lactose occurs when β-galactosidase activity levels are low but decreases as the β-galactosidase activities increase. The data indicate that bga1-encoded β-galactosidase activity is a critical factor for cellulase production on lactose.

Original languageEnglish
Pages (from-to)851-857
Number of pages7
JournalApplied and Environmental Microbiology
Volume71
Issue number2
DOIs
Publication statusPublished - 1 Feb 2005
MoE publication typeA1 Journal article-refereed

Fingerprint

Hypocrea
Galactosidases
galactosidases
Trichoderma reesei
Cellulase
Lactose
endo-1,4-beta-glucanase
lactose
protein
Cellulose 1,4-beta-Cellobiosidase
amino acid
cellulose 1,4-beta-cellobiosidase
gene expression
genomics
metabolism
arabinitol
Growth
gene
Galactitol
carbon

Cite this

Seiboth, B., Hartl, L., Salovuori, N., Lanthaler, K., Robson, G. D., Vehmaanperä, J., ... Kubicek, C. P. (2005). Role of the bga1-encoded extracellular β-galactosidase of Hypocrea jecorina in cellulase induction by lactose. Applied and Environmental Microbiology, 71(2), 851-857. https://doi.org/10.1128/AEM.71.2.851-857.2005
Seiboth, Bernhard ; Hartl, Lukas ; Salovuori, Noora ; Lanthaler, Karin ; Robson, Geoff D. ; Vehmaanperä, Jari ; Penttilä, Merja E. ; Kubicek, Christian P. / Role of the bga1-encoded extracellular β-galactosidase of Hypocrea jecorina in cellulase induction by lactose. In: Applied and Environmental Microbiology. 2005 ; Vol. 71, No. 2. pp. 851-857.
@article{278a82f4c6da4d499886c73e896b06cb,
title = "Role of the bga1-encoded extracellular β-galactosidase of Hypocrea jecorina in cellulase induction by lactose",
abstract = "Lactose is the only soluble and economically feasible carbon source for the production of cellulases or heterologous proteins regulated by cellulase expression signals by Hypocrea jecorina (Trichoderma reesei). We investigated the role of the major β-galactosidase of H. jecorina in lactose metabolism and cellulase induction. A genomic copy of the bga1 gene was cloned, and this copy encodes a 1,023-amino-acid protein with a 20-amino-acid signal sequence. This protein has a molecular mass of 109.3 kDa, belongs to glycosyl hydrolase family 35, and is the major extracellular β-galactosidase during growth on lactose. Its transcript was abundant during growth on L-arabinose and L-arabinitol but was much less common when the organism was grown on lactose, D-galactose, galactitol, D-xylose, and xylitol. Δbga1 strains grow more slowly and accumulate less biomass on lactose, but the cellobiohydrolase I and II gene expression and the final cellulase yields were comparable to those of the parental strain. Overexpression of bga1 under the control of the pyruvate kinase promoter reduced the lag phase, increased growth on lactose, and limited transcription of cellobiohydrolases. We detected an additional extracellular β-galactosidase activity that was not encoded by bga1 but no intracellular β-galactosidase activity. In conclusion, cellulase production on lactose occurs when β-galactosidase activity levels are low but decreases as the β-galactosidase activities increase. The data indicate that bga1-encoded β-galactosidase activity is a critical factor for cellulase production on lactose.",
author = "Bernhard Seiboth and Lukas Hartl and Noora Salovuori and Karin Lanthaler and Robson, {Geoff D.} and Jari Vehmaanper{\"a} and Penttil{\"a}, {Merja E.} and Kubicek, {Christian P.}",
year = "2005",
month = "2",
day = "1",
doi = "10.1128/AEM.71.2.851-857.2005",
language = "English",
volume = "71",
pages = "851--857",
journal = "Applied and Environmental Microbiology",
issn = "0099-2240",
publisher = "American Society for Microbiology",
number = "2",

}

Role of the bga1-encoded extracellular β-galactosidase of Hypocrea jecorina in cellulase induction by lactose. / Seiboth, Bernhard; Hartl, Lukas; Salovuori, Noora; Lanthaler, Karin; Robson, Geoff D.; Vehmaanperä, Jari; Penttilä, Merja E.; Kubicek, Christian P.

In: Applied and Environmental Microbiology, Vol. 71, No. 2, 01.02.2005, p. 851-857.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Role of the bga1-encoded extracellular β-galactosidase of Hypocrea jecorina in cellulase induction by lactose

AU - Seiboth, Bernhard

AU - Hartl, Lukas

AU - Salovuori, Noora

AU - Lanthaler, Karin

AU - Robson, Geoff D.

AU - Vehmaanperä, Jari

AU - Penttilä, Merja E.

AU - Kubicek, Christian P.

PY - 2005/2/1

Y1 - 2005/2/1

N2 - Lactose is the only soluble and economically feasible carbon source for the production of cellulases or heterologous proteins regulated by cellulase expression signals by Hypocrea jecorina (Trichoderma reesei). We investigated the role of the major β-galactosidase of H. jecorina in lactose metabolism and cellulase induction. A genomic copy of the bga1 gene was cloned, and this copy encodes a 1,023-amino-acid protein with a 20-amino-acid signal sequence. This protein has a molecular mass of 109.3 kDa, belongs to glycosyl hydrolase family 35, and is the major extracellular β-galactosidase during growth on lactose. Its transcript was abundant during growth on L-arabinose and L-arabinitol but was much less common when the organism was grown on lactose, D-galactose, galactitol, D-xylose, and xylitol. Δbga1 strains grow more slowly and accumulate less biomass on lactose, but the cellobiohydrolase I and II gene expression and the final cellulase yields were comparable to those of the parental strain. Overexpression of bga1 under the control of the pyruvate kinase promoter reduced the lag phase, increased growth on lactose, and limited transcription of cellobiohydrolases. We detected an additional extracellular β-galactosidase activity that was not encoded by bga1 but no intracellular β-galactosidase activity. In conclusion, cellulase production on lactose occurs when β-galactosidase activity levels are low but decreases as the β-galactosidase activities increase. The data indicate that bga1-encoded β-galactosidase activity is a critical factor for cellulase production on lactose.

AB - Lactose is the only soluble and economically feasible carbon source for the production of cellulases or heterologous proteins regulated by cellulase expression signals by Hypocrea jecorina (Trichoderma reesei). We investigated the role of the major β-galactosidase of H. jecorina in lactose metabolism and cellulase induction. A genomic copy of the bga1 gene was cloned, and this copy encodes a 1,023-amino-acid protein with a 20-amino-acid signal sequence. This protein has a molecular mass of 109.3 kDa, belongs to glycosyl hydrolase family 35, and is the major extracellular β-galactosidase during growth on lactose. Its transcript was abundant during growth on L-arabinose and L-arabinitol but was much less common when the organism was grown on lactose, D-galactose, galactitol, D-xylose, and xylitol. Δbga1 strains grow more slowly and accumulate less biomass on lactose, but the cellobiohydrolase I and II gene expression and the final cellulase yields were comparable to those of the parental strain. Overexpression of bga1 under the control of the pyruvate kinase promoter reduced the lag phase, increased growth on lactose, and limited transcription of cellobiohydrolases. We detected an additional extracellular β-galactosidase activity that was not encoded by bga1 but no intracellular β-galactosidase activity. In conclusion, cellulase production on lactose occurs when β-galactosidase activity levels are low but decreases as the β-galactosidase activities increase. The data indicate that bga1-encoded β-galactosidase activity is a critical factor for cellulase production on lactose.

UR - http://www.scopus.com/inward/record.url?scp=13544275588&partnerID=8YFLogxK

U2 - 10.1128/AEM.71.2.851-857.2005

DO - 10.1128/AEM.71.2.851-857.2005

M3 - Article

VL - 71

SP - 851

EP - 857

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

SN - 0099-2240

IS - 2

ER -