Combined use of growth rate correlated and growth rate independent promoters for recombinant glucoamylase production in Fusarium venenatum

Gordon, C.

doi:10.1016/s0378-1097(00)00535-8

Cited by 3 publications

(6 citation statements)

References 9 publications

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“…2b) meals were utilized by the fungi during incubation, resulting in residual sugar levels of 0.9-8.4 % w/w. A. pullulans (NRRL-Y-2311-1) and F. venenatum exhibited the lowest residual sugar levels on both [47] b [35] c [37] d [48] e [27] substrates, while M. circincelloides and T. reesei had the highest final levels of residual sugars. In the case of T. reesei, the higher than optimal final pH levels might explain why sugars were not more completely consumed [37].…”

Section: Residual Sugarsmentioning

confidence: 99%

Conversion of Canola Meal into a High‐Protein Feed Additive via Solid‐State Fungal Incubation Process

Croat

Berhow

Karki

et al. 2016

J Americ Oil Chem Soc

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further reduced GLS up to 99 and 98 %, respectively. Fiber levels increased due to the concentration effect of removing oligosaccharides and GLS. AbbreviationsADF Acid detergent fiber CP Cold-pressed dw Dry weight GLS Glucosinolate GYE Glucose yeast extract HE Hexane-extracted LC-MS Liquid chromatography-mass spectrometry NDF Neutral detergent fiber PDA Potato dextrose agar q-tof Quadrupole time-of-flight rpm Revolutions per minute RS Residual sugar RP-HPLC Reverse phase high performance liquid chromatography SLR Solid loading rate Abstract The study goal was to determine the optimal fungal culture to reduce glucosinolates (GLS), fiber, and residual sugars while increasing the protein content and nutritional value of canola meal. Solid-state incubation conditions were used to enhance filamentous growth of the fungi. Flask trials were performed using 50 % moisture content hexane-extracted (HE) or cold-pressed (CP) canola meal with incubation for 168 h at 30 °C. Incubation on HE canola meal Trichoderma reesei (NRRL-3653) achieved the greatest increase in protein content (23 %), while having the lowest residual levels of sugar (8 % w/w) and GLS (0.4 μM/g). Incubation on CP canola meal Trichoderma reesei (NRRL-3653), A. pullulans , and A. pullulans (NRRL-Y-2311-1) resulted in the greatest improvement in protein content (22.9, 16.9 and 15.4 %, respectively), while reducing total GLS content from 60.6 to 1.0, 3.2 and 10.7 μM/g, respectively. HE and CP canola meal GLS levels were reduced to 65.5 and 50.7 % by thermal treatments while solid-state microbial conversion Mark Berhow: Mention of trade names or commercial products in this paper is solely for the purpose of providing specific information and does not imply endorsement by the U.S. Department of Agriculture (USDA). The USDA is an equal opportunity provider and employer.

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Section: Residual Sugarsmentioning

confidence: 99%

Conversion of Canola Meal into a High‐Protein Feed Additive via Solid‐State Fungal Incubation Process

Croat

Berhow

Karki

et al. 2016

J Americ Oil Chem Soc

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“…A7 (4-8 mg GAM l À1 or 85-165 U GAM l À1 ) produced more GAM than A3/5 (1-2 mg GAM l À1 or 28-40 U GAM l À1 ) in batch culture (Fig. 4), and GAM production was similar to that of pIGF transformants of F. venenatum JeRS325 (Gordon et al 2001). It should not be necessary to produce recombinant F. solani f. sp.…”

Section: Resultsmentioning

confidence: 81%

“…This probably reflects poor expression of genes under the A. niger glaA promoter (Gordon et al 2001), which was used here to demonstrate the production of recombinant cutinase in F. venenatum A3/5 because the expression vector was readily available. A7 (4-8 mg GAM l À1 or 85-165 U GAM l À1 ) produced more GAM than A3/5 (1-2 mg GAM l À1 or 28-40 U GAM l À1 ) in batch culture (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Fusarium venenatum A3/5 was co-transformed with pIGF::CUT and pAN8-1 as described by Gordon et al (2001), using equal concentrations (10 mg) of pIGF::CUT and pAN8-1 with ca. 10 8 protoplasts.…”

Section: Fungal Transformationmentioning

confidence: 99%

“…pisi cutinase gene in Fusarium venenatum A3/5, a strain which has recently been developed for the production of other recombinant proteins (Royer et al 1995, Blinkovsky et al 1999. Although the Fusarium genus is diverse, F. venenatum A3/5 is able to correctly process a Fusarium oxysporum trypsin-like protease (Royer et al 1995) and is able to express genes under the control of promoters from F. oxysporum (trypsin-like protease promoter, Royer et al 1995) and Fusarium moniliforme (nitrate reductase promoter; Gordon et al 2001) and thus is likely to be a good host for cutinase production. It is also likely to correctly glycosylate the protein, unlike Escherichia coli or S. cerevisiae.…”

Section: Introductionmentioning

confidence: 99%

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Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5

2007

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Fusarium venenatum A3/5 was transformed using the Aspergillus niger expression plasmid, pIGF, in which the coding sequence for the F. solani f. sp. pisi cutinase gene had been inserted in frame, with a KEX2 cleavage site, with the truncated A. niger glucoamylase gene under control of the A. niger glucoamylase promoter. The transformant produced up to 21 U cutinase l(-1) in minimal medium containing glucose or starch as the primary carbon source. Glucoamylase (165 U l(-1) or 8 mg l(-1)) was also produced. Both the transformant and the parent strain produced cutinase in medium containing cutin.

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Food-processing enzymes from recombinant microorganisms—a review

Olempska-Beer

Merker

Ditto

et al. 2006

Regulatory Toxicology and Pharmacology

289

137

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Enzymes are commonly used in food processing and in the production of food ingredients. Enzymes traditionally isolated from culturable microorganisms, plants, and mammalian tissues are often not well-adapted to the conditions used in modern food production methods. The use of recombinant DNA technology has made it possible to manufacture novel enzymes suitable for specific food-processing conditions. Such enzymes may be discovered by screening microorganisms sampled from diverse environments or developed by modification of known enzymes using modern methods of protein engineering or molecular evolution. As a result, several important food-processing enzymes such as amylases and lipases with properties tailored to particular food applications have become available. Another important achievement is improvement of microbial production strains. For example, several microbial strains recently developed for enzyme production have been engineered to increase enzyme yield by deleting native genes encoding extracellular proteases. Moreover, certain fungal production strains have been modified to reduce or eliminate their potential for production of toxic secondary metabolites. In this article, we discuss the safety of microorganisms used as hosts for enzyme-encoding genes, the construction of recombinant production strains, and methods of improving enzyme properties. We also briefly describe the manufacture and safety assessment of enzyme preparations and summarize options for submitting information on enzyme preparations to the US Food and Drug Administration.

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Combined use of growth rate correlated and growth rate independent promoters for recombinant glucoamylase production in Fusarium venenatum

Cited by 3 publications

References 9 publications

Conversion of Canola Meal into a High‐Protein Feed Additive via Solid‐State Fungal Incubation Process

Conversion of Canola Meal into a High‐Protein Feed Additive via Solid‐State Fungal Incubation Process

Production of Fusarium solani f. sp. pisi cutinase in Fusarium venenatum A3/5

Food-processing enzymes from recombinant microorganisms—a review

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