Studies of β‐Glucoside‐ and Cellulose‐Splitting Enzymes from Different Strains of <i>Collybia velutipes</i>

Norkrans, Birgitta

doi:10.1111/j.1399-3054.1957.tb06965.x

Cited by 16 publications

(3 citation statements)

References 9 publications

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“…It is more heat labile than the other cellulase activities and can be selectively heat inactivated in extracts from the fungi Myrothecium iverrucuriu,22 Polyporus unnosus, 23 and Collybia ale-l~t i p e s , *~ whereas in Trichoderma it appears to be more heat sta-bIe. 17,24 In Aspergillus phoenicis, the half-life of p-glucosidase is 2 16 and 8.6 hr at 55 and 60"C, r e s p e c t i~e l y .~~…”

Section: Discussionmentioning

confidence: 99%

Saccharification of cellolulose by the cellulolytic enzyme system of Thermonospora sp. I. Stability of cellulolytic activities with respect to time, temperature, and pH

Hagerdal

Ferchak

Pye

1980

Biotech & Bioengineering

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PI? ilcidelp h iu , Pen n sy 1 L W n ici I 9 I 04 SummaryThe stabilities and optima with respect to temperature and pH of the P-glucosidase, Avicelase, and carboxymethylcellulase (CMCase) activities of Thermomonospora sp., in the culture filtrate, culture whole broth, and filtrate after sonication of culture solids, are reported. The P-glucosidase is cell associated and has an optimal activity at about pH 6.5 and 55°C. In the whole culture broth, it has a half-life of about 8 hr at 55°C and less than 1 hr at 60°C. while the half-life of the activity in the sonicated, cell-free filtrate is less than 1 hr at 55°C. The Avicelase and CMCase activities occur in the extracellular culture fluid and have optima at about pH 7.0 and 5.9, and 65 and 7O"C, respectively. The CMCase activity is stable over 24 hr at 60"C, but declines by 50% in the same period at 65°C. The Avicelase activity declines by 15% over 24 hr at 55°C. and by 50% at 60°C. The highest pH studied (pH 7.3) was the most destabilizing for all three activities. The thermostable characteristics of the cellulases from 7herniomonosporcr appear to make them suitable for commercial saccharification processes operating at elevated temperatures.

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Section: Discussionmentioning

confidence: 99%

Saccharification of cellolulose by the cellulolytic enzyme system of Thermonospora sp. I. Stability of cellulolytic activities with respect to time, temperature, and pH

Hagerdal

Ferchak

Pye

1980

Biotech & Bioengineering

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“…The reaction mixtures contained 60 μL of litter extract and 60 μL of a 5 mM PNPG solution in 50 mM sodium acetate buffer, and they were incubated at 50°C and pH 5 for 10 min as described by Norkrans (1957). The reactions were stopped by adding 120 μL of 1 M sodium carbonate solution, and the absorbance was measured at 400 nm using a microplate spectrophotometer (VersaMax, Molecular Devices Corporation, Sunnyvale, CA, USA).…”

Section: Methodsmentioning

confidence: 99%

Enzymatic Strategies and Carbon Use Efficiency of a Litter-Decomposing Fungus Grown on Maize Leaves, Stems, and Roots

et al. 2016

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Soil microorganisms can control the soil cycles of carbon (C), and depending on their C-use efficiency (CUE), these microorganisms either contribute to C stabilization in soil or produce CO2 when decomposing organic matter. However, little is known regarding the enzyme investment of microbial decomposers and the effects on their CUE. Our objective was to elucidate the strategies of litter-decomposing fungi as a function of litter quality. Fungal biosynthesis and respiration were accounted for by quantifying the investment in enzyme synthesis and enzyme efficiency. The basidiomycete Phanerochaete chrysosporium was grown on the leaves, stems, and roots of maize over 126 days in controlled conditions. We periodically measured the fungal biomass, enzyme activity, and chemical composition of the remaining litter and continuously measured the evolved C–CO2. The CUE observed for the maize litter was highest in the leaves (0.63), intermediate in the roots (0.40), and lowest in the stems (0.38). However, the enzyme efficiency and investment in enzyme synthesis did not follow the same pattern. The amount of litter C decomposed per mole of C-acquiring hydrolase activity was 354 μg C in the leaves, 246 μg C in the roots, and 1541 μg C in the stems (enzyme efficiency: stems > leaves > roots). The fungus exhibited the highest investment in C-acquiring enzyme when grown on the roots and produced 40–80% less enzyme activity when grown on the stems and leaves (investment in enzymes: roots > leaves > stems). The CUE was dependent on the initial availability and replenishment of the soluble substrate fraction with the degradation products. The production of these compounds was either limited because of the low enzyme efficiency, which occurred in the roots, or because of the low investments in enzyme synthesis, which occurred in the stems. Fungal biosynthesis relied on the ability of the fungus to invest in enzyme synthesis and the efficient interactions between the enzymes and the substrate. The investment decreased when N was limited, whereas the efficiency of the C-acquiring enzymes was primarily explained by the hemicellulose content and its embedment in recalcitrant lignin linkages. Our results are crucial for modeling microbial allocation strategies.

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“…Irpex lacteus (Nisizawa, 1955) and Poria vaillantii (Sison, Schubert & Nord, 1958) and the cellulase activity of different strains of some species compared, e.g. Elvingia applanata (Aoshima, 1954), Collybia velutipes (Norkrans, 1957).…”

Section: Introductionmentioning

confidence: 99%

Cellulase activity of Polyporus betulinus

Bell

Burnett

1966

Annals of Applied Biology

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S U M M A R YMethods are described for isolating and crossing monocaryons of P. betulinus and of determining their cellulase activity by observing changes in viscosity of a carboxy-methyl cellulose preparation.Cellulase activity, so measured, is not correlated with growth rate in the presence or absence of cellulose.Cellulase activity is almost certainly controlled polygenically and is inherited independently of mating type.X4-5 and 9; Y3-6 and 5. This indicates that cellulase activity is not profoundly affected by the parent mycelium in any one host or sporophore. It became a matter of

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Studies of β‐Glucoside‐ and Cellulose‐Splitting Enzymes from Different Strains of Collybia velutipes

Cited by 16 publications

References 9 publications

Saccharification of cellolulose by the cellulolytic enzyme system of Thermonospora sp. I. Stability of cellulolytic activities with respect to time, temperature, and pH

Saccharification of cellolulose by the cellulolytic enzyme system of Thermonospora sp. I. Stability of cellulolytic activities with respect to time, temperature, and pH

Enzymatic Strategies and Carbon Use Efficiency of a Litter-Decomposing Fungus Grown on Maize Leaves, Stems, and Roots

Cellulase activity of Polyporus betulinus

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