Structural Studies on Cutinase, a Glycoprotein Containing Novel Amino Acids and Glucuronic Acid Amide at the N Terminus

Lin, Tong‐Hong; Kolattukudy, Pappachan E.

doi:10.1111/j.1432-1033.1980.tb04580.x

Cited by 65 publications

(24 citation statements)

References 21 publications

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“…To date, the majority of the work has been done with a fungal pathogen of peas, Fusarium solani f. sp. pisi (Nectria haematococca) (Dantzig et al, 1986;Lin and Kolattukudy, 1980;Murphy et al, 1996;Purdy and Kolattukudy, 1975;Soliday and Kolattukudy, 1983).…”

Section: Introductionmentioning

confidence: 97%

“…Because cutinase plays an important role in virulence, several studies have been performed to elucidate its physiological and biochemical properties (Dantzig et al, 1986;Lin and Kolattukudy, 1980;Murphy et al, 1996;Purdy and Kolattukudy, 1975;Sebastian et al, 1987;Soliday and Kolattukudy, 1983). To date, the majority of the work has been done with a fungal pathogen of peas, Fusarium solani f. sp.…”

Section: Introductionmentioning

confidence: 98%

“…Some microorganisms have been shown to live on cutin as their sole carbon source and the production of extracellular cutinolytic enzymes has been presented (Lin and Kolattukudy, 1980;Purdy and Kolattukudy, 1975). Cutinases have been purified and characterized from several different sources, mainly fungi (Dantzig et al, 1986;Lin and Kolattukudy, 1980;Murphy et al, 1996;Petersen et al, 1997;Purdy and Kolattukudy, 1975) and pollen Sebastian et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

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Cutinase: From molecular level to bioprocess development

Carvalho¹,

Aires-Barros²,

Cabral³

1999

Biotechnol. Bioeng.

216

138

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Section: Introductionmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cutinase: From molecular level to bioprocess development

Carvalho¹,

Aires-Barros²,

Cabral³

1999

Biotechnol. Bioeng.

216

138

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“…Hydrolytic and synthetic reactions catalyzed by cutinase have potential use in the dairy industry for the hydrolysis of milk fat, in household detergents, in the oleochemical industry, in the synthesis of ingredients for personal-care products, and the synthesis of pharmaceuticals and agrochemicals containing one or more chiral centers [12]. To date, the majority of the work has been done with a fungal pathogen of peas, Fusarium solani f. pisi [13][14][15]. Production of cutinase from this fungus is commercially unviable and thus the genes are cloned and expressed in heterologous hosts.…”

Section: Introductionmentioning

confidence: 99%

Mixture design as a first step for optimization of fermentation medium for cutinase production from Colletotrichum lindemuthianum

Rispoli

Shah

2007

J Ind Microbiol Biotechnol

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Cutinase enzymes from fungi have found diverse applications in industry. However, most of the available literature on cutinase production is related to the cultivation of genetically engineered bacteria or yeast cells. In the present study, we use mixture design experiments to evaluate the influence of six nutrient elements on production of cutinase from the fungus Colletotrichum lindemuthianum. The nutritional elements were starch, glucose, ammonium sulfate, yeast extract, magnesium sulfate, and potassium phosphate. In the experimental design, we imposed the constraints that exactly one factor must be omitted in each set of experiments and no factor can account for more than one third of the mixture. Thirty different sets of experiments were designed. Results obtained showed that while starch is found to have negative influence on the production of the enzyme, yeast extract and potassium phosphate have a strong positive influence. Magnesium sulfate, ammonium sulfate, and glucose have low positive influence on the enzyme production. Contour plots have also been created to obtain information concerning the interaction effects of the media components on enzyme production.

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“…pisi live on cutin as their sole carbon source producing extracellular cutinases, and several bacterial cutinases (Pseudomonas putida, Pseudomonas mendocina, and Corynebacterium spp.) have been isolated and characterized (8,21,23,25,30,34,35). These enzymes have been largely exploited for esterification and transesterification in chemical synthesis (16) and have also been applied in the composition of laundry or dishwashing detergent (14,28,38).…”

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confidence: 99%

Enhanced Degradation of an Endocrine-Disrupting Chemical, Butyl Benzyl Phthalate, byFusarium oxysporumf. sp.pisiCutinase

Kim

Lee

Ahn

et al. 2002

Appl Environ Microbiol

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Compared to yeast esterase, fungal cutinase degraded butyl benzyl phthalate (BBP) far more efficiently; i.e., almost 60% of the BBP disappeared within 7.5 h. Also, the final chemical composition significantly depended on the enzyme used. Toxicity monitoring using bioluminescent bacteria showed that butyl methyl phthalate, a major product of degradation by esterase, was an oxidative toxic hazard.Phthalates are plasticizers used in the manufacture of polyvinyl chloride and often in paints, lacquers, and cosmetics (18,26,31). Phthalates found in sediment, water, and air (13) have also been detected in foods, as they can migrate out of food packaging materials (29,36). n-Butyl benzyl phthalate (BBP) is a phthalic ester in papers and paperboards used as packaging materials for aqueous, fatty, and dry foods (19,37). BBP exerted estrogenic activities in several in vitro tests (2,18,20,43). During the past 10 years, there have been a series of reports on the developmental toxicity of BBP in rats (1,11,12,39), and the teratogenic effects have also been observed in mice and chicks (4, 32).Cutinase, a hydrolytic enzyme that degrades cutin (a polyester consisting of hydroxy and epoxy fatty acids, usually with n-C 16 and n-C 18 of higher plants), can, unlike other lipases, show enzymatic activity without interfacial activation. Some microorganisms such as Fusarium oxysporum f. sp. pisi live on cutin as their sole carbon source producing extracellular cutinases, and several bacterial cutinases (Pseudomonas putida, Pseudomonas mendocina, and Corynebacterium spp.) have been isolated and characterized (8,21,23,25,30,34,35). These enzymes have been largely exploited for esterification and transesterification in chemical synthesis (16) and have also been applied in the composition of laundry or dishwashing detergent (14,28,38). Other potential uses for cutinase include its application in the oleochemistry industry (6) and in the degradation of plastic (22).In the present study, we investigated the efficacies of fungal cutinase and yeast esterase in the degradation of BBP. During the enzymatic degradation of BBP, time-course compositional changes of several BBP-derived compounds were monitored. The cellular toxicity of degradation products was also measured by using various bioluminescent bacteria.Enzymatic degradation of BBP by cutinase and esterase. Purified cutinase from F. oxysporum f. sp. pisi (kindly provided by C. M. J. Sagt, Utrecht University, Utrecht, The Netherlands) and commercial Candida cylindracea esterase (Boehringer Mannheim GmbH, Mannheim, Germany) were dissolved in Tris-HCl buffer (10 mM, pH 8.0), and the enzyme concentration was adjusted to 10 or 100 mg liter Ϫ1 . The enzymatic degradation of BBP (98% purity; Aldrich, Milwaukee, Wisc.) was begun by adding 50 l of the concentrated BBP solution (500 g liter Ϫ1 in pure methanol [99.9%; Merck, Darmstadt, Germany]) to 50 ml of the enzyme solution described above in a 250-ml flask and was continued for 3 days in the dark in a shaking incubator (30°C, 200 rpm).Analyses...

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Structural Studies on Cutinase, a Glycoprotein Containing Novel Amino Acids and Glucuronic Acid Amide at the N Terminus

Cited by 65 publications

References 21 publications

Cutinase: From molecular level to bioprocess development

Cutinase: From molecular level to bioprocess development

Mixture design as a first step for optimization of fermentation medium for cutinase production from Colletotrichum lindemuthianum

Enhanced Degradation of an Endocrine-Disrupting Chemical, Butyl Benzyl Phthalate, byFusarium oxysporumf. sp.pisiCutinase

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