Purification, characterization, and properties of β-glucosidase enzymes from Sclerotium rolfsii

Shewale, Jaiprakash G.; Sadana, J.C.

doi:10.1016/0003-9861(81)90024-2

Cited by 43 publications

(18 citation statements)

References 46 publications

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“…lactone in both species. Glucono-D-lactone has also been identified as a competitive inhibitor of β-1,4-glucosidase in previous studies (Scrivener and Slaytor, 1994;Shewale and Sadana, 1981;Santos and Terra, 1985). The inhibitory constant of glucono-D-lactone on β-1,4-glucosidase (K i ) was calculated using K m values from Table·2 and the equation: The activities of the enzymes in the digestive juice of both G. natalis and D. hirtipes were in the order laminarinase > licheninase > xylanase (Table·3).…”

Section: β-14-glucosidasementioning

confidence: 96%

“…After incubation, the absorbance of the samples was read at 445·nm. Cellulases of land crabs Glucono-D-lactone competitively inhibits β-1,4-glucosidase (Scrivener and Slaytor, 1994;Shewale and Sadana, 1981;Santos and Terra, 1985). The inhibitory constant of glucono-D-lactone on β-1,4-glucosidase was also determined by measuring β-1,4-glucosidase activity in the presence of 20·mmol·l Endo-β-1,4-glucanase.…”

Section: Measurement Of Enzyme Activities Cellulase Activitiesmentioning

confidence: 99%

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Presence and properties of cellulase and hemicellulase enzymes of the gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes

Linton¹,

Greenaway²

2004

Journal of Experimental Biology

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SUMMARY Digestive juice from the herbivorous gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes exhibited total cellulase activity and activities of two cellulase enzymes; endo-β-1,4-glucanase and β-1,4-glucosidase. These enzymes hydrolysed native cellulose to glucose. The digestive juice of both species also contained laminarinase,licheninase and xylanase, which hydrolysed laminarin, lichenin and xylan,respectively, to component sugars. The pH optima of β-1,4-glucosidase,endo-β-1,4-glucanase and total cellulase from G. natalis were 4–5.5, 5.5 and 5.5–7, respectively. In the digestive juice from D. hirtipes, the corresponding values were 4–7, 5.5–7 and 4–9, respectively. The pH of the digestive juice was 6.69±0.03 for G. natalis and 6.03±0.04 for D. hirtipes and it is likely that the cellulases operate near maximally in vivo. In G. natalis, total cellulase activity and endo-β-1,4-glucanase activity were higher than in D. hirtipes, and the former species can thus hydrolyse cellulose more rapidly. β-1,4-glucosidase from G. natalis was inhibited less by glucono-d-lactone(Ki=11.12 mmol l-1) than was theβ-1,4-glucosidase from D. hirtipes (Ki=4.53 mmol l-1). The greater resistance to inhibition by theβ-1,4-glucosidase from G. natalis may contribute to the efficiency of the cellulase system in vivo by counteracting the effects of product inhibition and possibly dietary tannins. The activity ofβ-1,4-glucosidase in the digestive juice of D. hirtipes was higher than that of G. natalis.

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Section: β-14-glucosidasementioning

confidence: 96%

Section: Measurement Of Enzyme Activities Cellulase Activitiesmentioning

confidence: 99%

Presence and properties of cellulase and hemicellulase enzymes of the gecarcinid land crabs Gecarcoidea natalis and Discoplax hirtipes

Linton¹,

Greenaway²

2004

Journal of Experimental Biology

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“…However, CreA homologs have been detected in all basidiomycete genomes sequenced so far (184). In line with the ascomycetes, various basidiomycetes, such as the white rot fungus Trametes (Coriolus) versicolor, the litter decomposers A. bisporus and V. volvacea, the phytopathogen S. rolfsii, and the basidiomycete yeast Rhodotorula minuta, have CAZyme-encoding genes that are repressed by glucose and other monosaccharides (89,(185)(186)(187)(188). Some CAZymeencoding genes are also repressed by monosaccharides that seem unrelated to the enzymes that these genes encode.…”

Section: Repression Of Gene Expression In Basidiomycetesmentioning

confidence: 99%

Plant-Polysaccharide-Degrading Enzymes from Basidiomycetes

Rytioja

Hildén

Yuzon

et al. 2014

Microbiol Mol Biol Rev

355

287

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SUMMARY Basidiomycete fungi subsist on various types of plant material in diverse environments, from living and dead trees and forest litter to crops and grasses and to decaying plant matter in soils. Due to the variation in their natural carbon sources, basidiomycetes have highly varied plant-polysaccharide-degrading capabilities. This topic is not as well studied for basidiomycetes as for ascomycete fungi, which are the main sources of knowledge on fungal plant polysaccharide degradation. Research on plant-biomass-decaying fungi has focused on isolating enzymes for current and future applications, such as for the production of fuels, the food industry, and waste treatment. More recently, genomic studies of basidiomycete fungi have provided a profound view of the plant-biomass-degrading potential of wood-rotting, litter-decomposing, plant-pathogenic, and ectomycorrhizal (ECM) basidiomycetes. This review summarizes the current knowledge on plant polysaccharide depolymerization by basidiomycete species from diverse habitats. In addition, these data are compared to those for the most broadly studied ascomycete genus, Aspergillus , to provide insight into specific features of basidiomycetes with respect to plant polysaccharide degradation.

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“…The synergistic effect was expressed as in Table II of f3-glucosidase-3 was not affected by albumin. It was found that the f3-glucosidase of Sclerotium ro/fsii 14 ) was stabilized by albumin. The optimum pHs of f3-glucosidase-l and -2 were 4.0",4.5, resembling those of f3-glucosidases from various fungi.…”

Section: Discussionmentioning

confidence: 99%