Construction of a yeast vector directing the synthesis and release of barley (1→3, 1→4)-β-glucanase

Jackson, Elizabeth A.; Ballance, G. M.; Thomsen, Kristine Rømer

doi:10.1007/bf02907317

Cited by 36 publications

(6 citation statements)

References 37 publications

(27 reference statements)

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“…During germination as well as malting in the brewhouse, ␤-glucanase isoenzymes are secreted from the aleurone and scutellum and released into the endosperm. With the aim of constructing a glucanolytic brewing yeast strain, the ␤-1,3-1,4-glucanase gene from barley was cloned and expressed in S. cerevisiae (308). This gene was fused in frame to the signal sequences of the mouse ␣-amylase, yeast PHO5-encoded phosphatase, and SUC2-encoded invertase (504).…”

Section: Heterologous Cellulase Expression In Bacteriamentioning

confidence: 99%

Microbial Cellulose Utilization: Fundamentals and Biotechnology

Lynd

Weimer

Zyl³

et al. 2002

Microbiol Mol Biol Rev

3,931

2,868

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Fundamental features of microbial cellulose utilization are examined at successively higher levels of aggregation encompassing the structure and composition of cellulosic biomass, taxonomic diversity, cellulase enzyme systems, molecular biology of cellulase enzymes, physiology of cellulolytic microorganisms, ecological aspects of cellulase-degrading communities, and rate-limiting factors in nature. The methodological basis for studying microbial cellulose utilization is considered relative to quantification of cells and enzymes in the presence of solid substrates as well as apparatus and analysis for cellulose-grown continuous cultures. Quantitative description of cellulose hydrolysis is addressed with respect to adsorption of cellulase enzymes, rates of enzymatic hydrolysis, bioenergetics of microbial cellulose utilization, kinetics of microbial cellulose utilization, and contrasting features compared to soluble substrate kinetics. A biological perspective on processing cellulosic biomass is presented, including features of pretreated substrates and alternative process configurations. Organism development is considered for “consolidated bioprocessing” (CBP), in which the production of cellulolytic enzymes, hydrolysis of biomass, and fermentation of resulting sugars to desired products occur in one step. Two organism development strategies for CBP are examined: (i) improve product yield and tolerance in microorganisms able to utilize cellulose, or (ii) express a heterologous system for cellulose hydrolysis and utilization in microorganisms that exhibit high product yield and tolerance. A concluding discussion identifies unresolved issues pertaining to microbial cellulose utilization, suggests approaches by which such issues might be resolved, and contrasts a microbially oriented cellulose hydrolysis paradigm to the more conventional enzymatically oriented paradigm in both fundamental and applied contexts

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Section: Heterologous Cellulase Expression In Bacteriamentioning

confidence: 99%

Microbial Cellulose Utilization: Fundamentals and Biotechnology

Lynd

Weimer

Zyl³

et al. 2002

Microbiol Mol Biol Rev

3,931

2,868

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“…We have found similar purine-rich regions in barley, rice and wheat cc-amylase untranslated leaders that are expressed in the germinating seeds under the regulation of gibberellins. There is very little sequence similarity between the untranslated nucleotide sequence in the 3' end of AHV29 and that of isozyme I1 [6].…”

Section: Aminomentioning

confidence: 99%

The isolation and characterization of a barley 1,3‐1,4‐β‐glucanase gene

Litts¹,

Simmons²,

Karrer³

et al. 1990

European Journal of Biochemistry

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The barley gene encoding isozyme I of 1,3‐1,4‐β‐glucanase was isolated and sequenced. The 6260‐bp region sequenced included 1885 bp of the 5′‐flanking region, the entire coding region, an intron of 2490 bp, and 792 bp of the 3′‐flanking region. The 1,3‐1,4‐β‐glucanase mRNA was found to be regulated at the level of RNA accumulation by both gibberellins (positively) and abscisic acid (negatively) in barley aleurones. The mRNA for isozyme II preferentially accumulated (70%) relative to the mRNA for isozyme I (30%) in poly(A)‐rich RNA isolated from material including both the aleurone and the scutellum tissues. The gene family encoding 1,3‐1,4‐β‐glucanase enzymes in barley was found to be comprised of two closely related genes, isozymes I and II, as well as several related sequences that could be identified by Southern blot analysis. The nucleotide sequence for the 5′ untranslated leader and the coding region for the signal peptide of the isozyme II transcript were determined from a cDNA produced by the polymerase chain reaction. The structure of the protein encoded by the isozyme I gene is also discussed.

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“…Ampicillin was used in a concentration of 100 ~tg/ml. Saccharomyces cerevisiae cells of strain DBY746 (16) were cultured in either YPD or synthetic complete (SC) media (26). Barley l~-glucan in a concentration of 0.1% (w/v) added to SC medium permitted the selection of yeast cells secreting []-glucanase by utilizing Congo red as indicator for the presence or absence of ~-glucan around the colony (16).…”

Section: Microbial Strains and Culture Mediamentioning

confidence: 99%

“…In order to fuse the two double-stranded oligonucleotides encoding the signal peptides for yeast invertase and yeast acid phosphatase 5 onto the most distal 5' ApaI-cut end of the 13-glucanase gene (16), the BamHI-PstI fragment containing a part of the barley ~glucanase gene from plasmid pYBAGI7 (16) was cloned into the BamHI-PstI cut cloning vector pTZ19R thereby creating the plasmid pAG which then was cut with BamHI and ApaI. The large fragment was purified and ligated with the doublestranded oligonucleotides with ApaI and BamHI compatible ends giving rise to plasmid pP5 (modified phosphatase signal code) and plasmid pI5 (invertase signal code).…”

Section: Plasmid Constructionsmentioning

confidence: 99%

“…2) was constructed by ligation of the small blunt ended EcoRI fragment (containing the mouse a-amylase signal peptide code fused in frame with the 13-glucanase structural gene behind the PGK promoter) from pYBAGI 7 into the BglII digested and blunt ended pMAl9. Plasmid pYBAG 17 has been described (16). Expression-secretion cassettes used in this study are listed in Table I.…”

Section: Plasmid Constructionsmentioning

confidence: 99%

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