Purification and characterization of a Coffea canephora α-D-galactosidase isozyme

Haibach, Frederick G.; Hata, Junichi; Mitra, Moonmoon; Dhar, M; Harmata, Michael; Sun, Peng; Smith, Daniel

doi:10.1016/0006-291x(91)92117-3

Cited by 23 publications

(12 citation statements)

References 13 publications

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“…Analysis of α-D-galactosidase expression: α-D-galactosidase (α-Gal; EC 3.2.1.22) is a very abundant protein in mature coffee beans (see Sigma-Aldrich catalog ref G8507) and was one of the first plant α-D-galactosidases to be characterized (Courtois and Petek, 1966;Carchon and De Bruyne, 1975;Haibach et al, 1991). It acts on galactomannans by removing galactose residues at the O-6 position of the (1→4)-β-man- and "endosperm phase (En)" (≈ 120 DAF up to the harvest).…”

Section: Genes Coding For Storage Proteinsmentioning

confidence: 99%

Cytology, biochemistry and molecular changes during coffee fruit development

Castro

Marraccini

2006

Braz. J. Plant Physiol.

134

130

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In commercial coffee species (Coffea arabica and Coffea canephora), fruit development is a lengthy process, characterized by tissue changes and evolutions. For example, soon after fecundation and up to mid development, the fruit is mainly constituted of the pericarp and perisperm tissue. Thereafter, the perisperm gradually disappears and is progressively replaced by the endosperm (true seed). Initially present in a "liquid" state, the endosperm hardens as it ripens during the maturation phase, as a result of accumulation of storage proteins, sucrose and complex polysaccharides representing the main reserves of the seed. The last step of maturation is characterized by the dehydration of the endosperm and the color change of the pericarp. Important quantitative and qualitative changes accompany fruit growth, highlighting the importance of its study to better understand the final characteristics of coffee beans. Following a description of the coffee fruit tissues, this review presents some data concerning biochemical, enzymatic and gene expression variations observed during the coffee fruit development. The latter will also be analyzed in the light of recent data (electronic expression profiles) arising from the Brazilian Coffee Genome Project. Key words: Coffea spp, bean development, cell cycle, endosperm, EST, gene expression, pericarp, perisperm.Cytology, biochemistry and molecular changes during coffee fruit development: Em espécies comerciais de café (Coffea arabica e Coffea canephora), o desenvolvimento do fruto de café é um processo longo, caracterizado por mudanças e evoluções nos tecidos. Por exemplo, logo após a fecundação e até a metade do desenvolvimento, o fruto é principalmente constituído pelo pericarpo e perisperma. Em seguida, o perisperma gradualmente desaparece e é progressivamente substituído pelo endosperma (semente verdadeira). Inicialmente o endosperma apresenta-se no estado "líquido", o endosperma endurece durante a fase de maturação, como resultado do acúmulo gradual de proteínas de reserva, sacarose e polissacarídeos complexos representando as principais reservas da semente. O último passo da maturação é caracterizado pela desidratação do endosperma e pela mudança de cor do pericarpo. Importantes alterações quantitativas e qualitativas acompanham o crescimento do fruto, ilustrando a importância do seu estudo para melhor compreender as características finais das sementes de café. Seguindo a descrição dos tecidos do fruto de café, esta revisão apresenta alguns dados relativos às variações bioquímicas, enzimáticas e de expressão gênica durante o desenvolvimento do fruto. A expressão de genes será também analisada em função de dados recentes (perfil de expressão eletrônica) oriundos do Projeto Genoma Brasileiro Café. Palavras-chave: Coffea spp, ciclo celular, desenvolvimento da semente, endosperma, EST, expressão gênica, pericarpo, perisperma. INTRODUCTIONThe Coffea genus contains around 100 species (Charrier and Berthaud, 1985). Within these species, C. arabica (Arabica) and C. canephora (Rob...

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Section: Genes Coding For Storage Proteinsmentioning

confidence: 99%

Cytology, biochemistry and molecular changes during coffee fruit development

Castro

Marraccini

2006

Braz. J. Plant Physiol.

134

130

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“…Several lysosomal exoglycosidases have demonstrated this effect on human erythrocytes (Goldstein et al, 1982;Haibach et al, 1991). Several lysosomal exoglycosidases have demonstrated this effect on human erythrocytes (Goldstein et al, 1982;Haibach et al, 1991).…”

Section: Introductionmentioning

confidence: 89%

Blood Group B Degrading Activity ofRuminococcus gnavusα-Galactosidase

Hata

Smith

2004

Artificial Cells, Blood Substitutes, and Biotechnology

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Ruminococcus gnavus is a Gram positive, nonspore-forming obligate anaerobe normally found in the human alimentary tract. In culture, this organism constitutively produces a 1-3 alpha-galactosidase. We fractionated and characterized this enzyme demonstrating hydrolysis of the B epitope on erythrocyte membranes and seroconversion to H epitope (blood type O). Since the enzyme yield was low, cell suspension studies could not be performed. Instead, hydrolysis of the B membrane epitope was studied with an ELISA. A highly purified enzyme product was analyzed for characteristics such as pH, ionic strength, and temperature optimum. Activity in red cell preservative solutions and in the presence of type B plasma was also demonstrated. Ruminococcus gnavus a 1-3 alpha-galactosidase has potential application in the enzymatic conversion of type B to O packed red blood cell units.

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“…For lysoGb3 8 different concentrations of the lipid, ranging from 2 to 200 μM, were incubated with 2.5 μg/mL of A1.1 and Fabrazyme for 45 min at 37 o C. LC-MC/MS was used to measure glycosphingoid bases (lyso-glycosphingolipids), as previously described (30,49). As internal standard 13 Clyso-Gb3 was used (30). Kinetics parameters K m and k cat were determined at pH 4.5, using GraphPad Prism7 for calculations.…”

Section: Activity Towards Lipid Substratesmentioning

confidence: 99%

“…One of the first plant α-galactosidases to be cloned and biochemically characterized was an enzyme from coffee beans (11). It occurs as two different isoforms with molecular weights of 28 kDa and 36.5 kDa showing slightly different pH optima (pH 5.3 and 6.3) and isoelectric points (12,13). Similar heterogeneity of α-galactosidases exists in other plant species, for example in rice (6).…”

Section: Introductionmentioning

confidence: 99%