A Modified Preparation of the Universal Buffer Described by Teorell and Stenhagen

Östling, Sven; Virtama, P

doi:10.1111/j.1748-1716.1946.tb00349.x

Cited by 38 publications

(14 citation statements)

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“…Total oxidative enzyme assays were completed using 25 mM L-DOPA +0.3% hydrogen peroxide (Saiya-Cork et al, 2002 ). Slurry was prepared by vortexing 2 g of beads in 40 ml pH 4.7 Modified Universal Buffer (Östling and Virtama, 1946 ). An equal volume of substrate was added to each well.…”

Section: Methodsmentioning

confidence: 99%

Two decades of warming increases diversity of a potentially lignolytic bacterial community

2015

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As Earth's climate warms, the massive stores of carbon found in soil are predicted to become depleted, and leave behind a smaller carbon pool that is less accessible to microbes. At a long-term forest soil-warming experiment in central Massachusetts, soil respiration and bacterial diversity have increased, while fungal biomass and microbially-accessible soil carbon have decreased. Here, we evaluate how warming has affected the microbial community's capability to degrade chemically-complex soil carbon using lignin-amended BioSep beads. We profiled the bacterial and fungal communities using PCR-based methods and completed extracellular enzyme assays as a proxy for potential community function. We found that lignin-amended beads selected for a distinct community containing bacterial taxa closely related to known lignin degraders, as well as members of many genera not previously noted as capable of degrading lignin. Warming tended to drive bacterial community structure more strongly in the lignin beads, while the effect on the fungal community was limited to unamended beads. Of those bacterial operational taxonomic units (OTUs) enriched by the warming treatment, many were enriched uniquely on lignin-amended beads. These taxa may be contributing to enhanced soil respiration under warming despite reduced readily available C availability. In aggregate, these results suggest that there is genetic potential for chemically complex soil carbon degradation that may lead to extended elevated soil respiration with long-term warming.

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Section: Methodsmentioning

confidence: 99%

Two decades of warming increases diversity of a potentially lignolytic bacterial community

2015

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“…A stock solution of 0.5% (w/v) -carrageenan (Danisco) was prepared in 50 mM MOPS, pH 7, 150 mM NaCl for PcCgkA GH16 and its mutants, in Teorell buffer (60) to determine the best range of pH for both construction of ZgCgkA GH16 and then in 50 mM MES, pH 6, 300 mM NaCl for the determination of kinetic constants. Aliquots (14 l) of enzyme at the appropriate concentration were incubated in triplicate in the presence of -carrageenan solution (126 l) at a final concentration of 0.125% (w/v) at 40°C.…”

Section: Enzymatic Activity Assays On -Carrageenan By Reducing Sugar mentioning

confidence: 99%

Structural insights into marine carbohydrate degradation by family GH16 κ-carrageenases

Matard-Mann¹,

Bernard²,

Leroux³

et al. 2017

Journal of Biological Chemistry

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Carrageenans are sulfated α-1,3-β-1,4-galactans found in the cell wall of some red algae that are practically valuable for their gelation and biomimetic properties but also serve as a potential carbon source for marine bacteria. Carbohydrate degradation has been studied extensively for terrestrial plant/bacterial systems, but sulfation is not present in these cases, meaning the marine enzymes used to degrade carrageenans must possess unique features to recognize these modifications. To gain insights into these features, we have focused on κ-carrageenases from two distant bacterial phyla, which belong to glycoside hydrolase family 16 and cleave the β-1,4 linkage of κ-carrageenan. We have solved the crystal structure of the catalytic module of CgkA from at 1.66 Å resolution and compared it with the only other structure available, that of CgkA from 9 (ATCC 43555). We also describe the first substrate complex in the inactivated mutant form of CgkA at 1.7 Å resolution. The structural and biochemical comparison of these enzymes suggests key determinants that underlie the functional properties of this subfamily. In particular, we identified several arginine residues that interact with the polyanionic substrate, and confirmed the functional relevance of these amino acids using a targeted mutagenesis strategy. These results give new insight into the diversity of the κ-carrageenase subfamily. The phylogenetic analyses show the presence of several distinct clades of enzymes that relate to differences in modes of action or subtle differences within the same substrate specificity, matching the hybrid character of the κ-carrageenan polymer.

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“…MM agar plates containing acetamide as sole nitrogen source were made as described previously (Kelly and Hynes, 1985). Setting the pH of MM within a range of 5-9 was accomplished by using a phosphate-citrate-borate-, a citrate-phosphate-, or a phosphate-buffer (Gomori, 1948;McIlvaine, 1921;Ostling and Virtama, 1946). Transformation of A. niger was performed as described .…”

Section: Strains Plasmids Cosmids and Growth Conditionsmentioning

confidence: 99%

Vacuolar H+-ATPase plays a key role in cell wall biosynthesis of Aspergillus niger

Schachtschabel

Arentshorst

Lagendijk

2012

Fungal Genetics and Biology

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A Modified Preparation of the Universal Buffer Described by Teorell and Stenhagen

Cited by 38 publications

References 1 publication

Two decades of warming increases diversity of a potentially lignolytic bacterial community

Two decades of warming increases diversity of a potentially lignolytic bacterial community

Structural insights into marine carbohydrate degradation by family GH16 κ-carrageenases

Vacuolar H+-ATPase plays a key role in cell wall biosynthesis of Aspergillus niger

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