The glucose oxidase of Penicillium variabile P16: gene cloning, sequencing and expression

Pulci, V.; D’Ovidio, R.; Petruccioli, Maurizio; Federici, Federico

doi:10.1111/j.1472-765x.2004.01470.x

Cited by 17 publications

(10 citation statements)

References 15 publications

(31 reference statements)

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“…Conversely, the intracellular rGOD activity of Penicillium variabile P16 was maximum (4·30 U ml −1 ) after 36 h of fermentation, while the extracellular one was highest (8·05 U ml −1 ) at the 96th hour (Pulci et al . ).…”

Section: Resultsmentioning

confidence: 97%

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Production and characterization of recombinant glucose oxidase from Aspergillus niger expressed in Pichia pastoris

Meng

Zhao

Yang

et al. 2014

Lett Appl Microbiol

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Significance and Impact of Study: Glucose oxidase is a very important enzyme produced by several species. However, large-scale applications have always been postponed by its complexity in fermentation and purification. Our research focused on developing new purification strategy of recombinant GOD from A. niger expressed in P. pastoris. Here, we described this novel one-step purification method and subsequent research in the characteristics of rGOD which showed different results from previous work. These can open new opportunities to increase its application. AbstractRecombinant glucose oxidase from Aspergillus niger expressed in Pichia pastoris by fed-batch fermentation was purified and assessed with 1Á26 purification fold to homogeneity using Q-Sepharose F.F. chromatography. The enzyme was determined by SDS-PAGE and gradient PAGE, which showed a dimeric form of 150 kDa. The purified rGOD was proved to be a glycoprotein, and the content of which was estimated to be 36Á7 and 25Á14% by phenol-sulfuric acid and anthrone-sulfuric acid methods. Characteristics demonstrated that the highest activity was in pH 6Á0 at 40°C and was stable at a broad pH range from 4Á0 to 9Á0 at 55°C or below. The optimum substrate for this enzyme was D-glucose, and the K m was 21Á06 mmol l À1 as well as the V max was 359 lmol min À1 mg À1 .rGOD possessed high resistance to various chemicals except for Hg 2+ , Fe 2+, Ag + , Cu 2+ , 1,4-dithiothreitol, sodium dodecyl sulfate and ascorbic acid. In addition, the inhibitors also exhibited intensive fluorescence quenching effect on rGOD.

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Section: Resultsmentioning

confidence: 97%

“…) and Pichia pastoris (Pulci et al . ). The methylotrophic yeast P. pastoris has been proved successfully due to its powerful and tightly regulated methanol‐inducible alcohol oxidase 1 promoter (AOX 1) and its capacity for exogenous protein secretion (Macauley‐Patrick et al .…”

Section: Introductionmentioning

confidence: 97%

Production and characterization of recombinant glucose oxidase from Aspergillus niger expressed in Pichia pastoris

Meng

Zhao

Yang

et al. 2014

Lett Appl Microbiol

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“…Same letters above column represent nonsignificant difference between treatments, while different letters represent significant differences (LSD, ANOVA, P < 0.05). Stosz et al, 1996;Murray et al, 1997;Rando et al, 1997;Liu et al, 1998;Pulci et al, 2004). GOX activities have been detected in insect species such as A. mellifera (Ohashi et al, 1999), H. zea (Eichenseer et al, 1999), S. exigua (Merkx-Jacques and Bede, 2004;Merkx-Jacques and Bede, 2005), Mamestra configurata (Merkx-Jacques and Bede, 2004), H. armigera, and H. assulta (Zong and Wang, 2004), and recently were extensively investigated in 85 species of Lepidoptera and three species of plant-feeding Hymenoptera (Eichenseer et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

CHARACTERIZATION OF GLUCOSE‐INDUCED GLUCOSE OXIDASE GENE AND PROTEIN EXPRESSION IN Helicoverpa armigera LARVAE

Tang

Kang

et al. 2012

Arch Insect Biochem Physiol

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Caterpillar labial salivary enzyme glucose oxidase (GOX) plays an important role in plant-insect interactions by suppressing the caterpillar-induced nicotine production in tobacco plants. In the present study, we cloned and characterized the GOX gene (HaGox) from labial salivary glands of Helicoverpa armigera larvae using 3' and 5' RACE, homologous analysis, phylogenetic analysis, LC-MS/MS, and qRT-PCR. The deduced GOX amino acid sequence (606 amino acids) shares 99% and 76% identity with H. zea and Spodoptera exigua GOX, respectively, and is consistent with the GOX protein sequence identified from H. armigera labial salivary gland. These results confirmed that the HaGox encode the GOX protein. Transcript levels of HaGox in larval labial salivary glands were significantly higher than those in midgut and hemolymph, respectively, and those of caterpillars reared on tobacco leaves coated with 0.1%, 1%, and 10% glucose solutions were significantly higher than those reared on 0.01% glucose-coated leaves or control tobacco leaves. Western blot and native PAGE showed that GOX protein expression levels and GOX enzymatic activities also increased with dietary glucose. These results proved that GOX expressions in larval labial salivary glands induced by dietary glucose were exhibited not only on transcriptional levels, but also on translational/posttranslational levels.

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“…The purpose of their mutation and expression in different organisms was to increase enzyme yield, facilitate enzyme purification, increase specific activity, improve the enzyme stability, and enhance selectivity for glucose. [24][25][26][27][28][29][30][31][32][33][34][35] The two enzyme families differ in their redox potentials, the strengths of the bonds between their protein-devoid apoenzymes and their cofactors, their cosubstrates, their turnover rates, their Michaelis constants (K m ), and their selectivity for glucose.…”

Section: The Enzymes Of Glucose Electrooxidizing Anodesmentioning

confidence: 99%

Electrochemical Glucose Sensors and Their Applications in Diabetes Management

2008

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About 6,000 peer reviewed articles have been published on electrochemical glucose assays and sensors, of which 700 were published in the 2005-2006 two-year period. Their number makes a full review of the literature, or even of the most recent advances, impossible. Nevertheless, this review should acquaint the reader with the fundamentals of the electrochemistry of glucose and provide a perspective of the evolution of the electrochemical glucose assays and monitors helping diabetic people, who constitute about 5% of the world's population. Because of the large number of diabetic people, no assay is performed more frequently than that of glucose. Most of these assays are electrochemical. The reader interested also in nonelectrochemical assays used in, or proposed for, the management of diabetes is referred to a 2007 review of Kondepati and Heise. 1 Adam Heller was born in 1933. Surviving the Holocaust, he arrived in Israel in 1945. He received his M.Sc. in Chemistry and Physics in 1957, then his PhD in Organic Chemistry in 1961 from Ernst David Bergman at the Hebrew University in Jerusalem. He postdoced at UC Berkeley (1962-3) and at Bell Laboratories . At GTE Labs (1964-1975 he built the first Nd 3+ liquid laser and, with J. J. Auborn, the still worldwide used Li/SOCl 2 battery. At Bell Labs (1975)(1976)(1977)(1978)(1979)(1980)(1981)(1982)(1983)(1984)(1985)(1986)(1987)(1988) he designed the first >10% efficient electrochemical solar cells and the first >10% efficient hydrogengenerating solar-powered photoelectrode. He also headed Bell Labs' Electronic Materials Research Department (1977)(1978)(1979)(1980)(1981)(1982)(1983)(1984)(1985)(1986)(1987)(1988), which developed part of the high density chip interconnection technology underlying the miniaturization of portable electronic devices. He was appointed to the Ernest Cockrell Sr. Chair in Engineering of the University of Texas at Austin in 1988, and in 2001 became one of UT's first Research Professors. At UT he pioneered the electrical wiring of enzymes. In 1996 he cofounded with his son Ephraim Heller TheraSense Inc., now part of Abbott Diabetes Care, to improve the lives of diabetic people. The company introduced in 2000 the blood sugar monitor FreeStyle, a thin-layer microcoulometer utilizing only 300 nL of blood, so little that it was, for the first time, painlessly obtained. In 2007 it provided for more than 1 billion painless glucose assays. After alleviating the pain of diabetes monitoring, FreeStyle Navigator, based on the electrical wiring of glucose oxidase, introduced in 2007 in Europe and Israel and in 2008 in the U.S., removed the worry of diabetic people by continuously monitoring their glucose levels. Heller aims his work at alleviating suffering through bioelectrochemistry.

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The glucose oxidase of Penicillium variabile P16: gene cloning, sequencing and expression

Cited by 17 publications

References 15 publications

Production and characterization of recombinant glucose oxidase from Aspergillus niger expressed in Pichia pastoris

Production and characterization of recombinant glucose oxidase from Aspergillus niger expressed in Pichia pastoris

CHARACTERIZATION OF GLUCOSE‐INDUCED GLUCOSE OXIDASE GENE AND PROTEIN EXPRESSION IN Helicoverpa armigera LARVAE

Electrochemical Glucose Sensors and Their Applications in Diabetes Management

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