Isolation and characterization of a 1,4-beta-D-glucan glucohydrolase from the yeast, Torulopsis wickerhamii.

Himmel, Michael E.; Tucker, Melvin P.; Lastick, Stanley M.; Oh, Kyeong Keun; Fox, James W.; Spindler, Diane D.; Grohmann, K.

doi:10.1016/s0021-9258(18)69254-3

Cited by 17 publications

(1 citation statement)

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“…These enzymes include both 1,4- p - d -glucan glucohydrolases (EC 3.2.1.74) as well as 1,4- p - d -glucan cellobiohydrolase (EC 3.2.1.91). 10 Cellobiohydrolases generally cleave the cellulose strand by attaching to the ends of microfibrils and results in the production of cellobiose. Mostly these enzymes belong to glycoside hydrolase family six, seven and nine, however, some of these enzymes also found in GH-48 and GH-5.…”

Section: Introductionmentioning

confidence: 99%

Efficient biomass saccharification using a novel cellobiohydrolase from Clostridium clariflavum for utilization in biofuel industry

et al. 2021

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Section: Introductionmentioning

confidence: 99%

Efficient biomass saccharification using a novel cellobiohydrolase from Clostridium clariflavum for utilization in biofuel industry

et al. 2021

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Characterization of a cellodextrin glucohydrolase with soluble oligomeric substrates: Experimental results and modeling of concentration‐time‐course data

Schmid

Wandrey

1989

Biotech & Bioengineering

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A previously isolated cellodextrin glucohydrolase (beta-glucosidase) from Trichoderma reesei QM 9414 is characterized using beta-1,4-glucose oligomers with defined degrees of polymerization as soluble substrates. The enzyme splits off glucose units from the nonreducing chain ends of cellooligomers. Besides this hydrolytic activity there is also evidence for transfer activity depending on the concentration and degree of polymerization of substrates. Concentration-time-course data have been gathered for the degradation of cellobiose, cellotriose, cellotetraose, cellopentaose, and cellohexaose covering a wide range of enzyme and substrate concentrations. A Michaelis-Menten type kinetic model has been developed, which is able to satisfactorily describe the complex system of parallel and series reactions during the conversion of oligomers to glucose. The only kind of inhibition considered is competitive inhibition by the final product glucose. The model takes into account the formation of multiple enzyme-substrate complexes and is limited to those conditions, in which no transglucosylation products are observed. Cellodextrins with higher degrees of polymerization are found to be better substrates for this enzyme than is the dimer cellobiose.

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How to calculate thermostability of enzymes using a simple approach

Saqib

Siddiqui

2018

Biochem Molecular Bio Educ

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Determination of thermostability of enzymes is of prime importance for their successful industrial applications and, yet, the published data has often been incompletely analyzed to assess the suitability of enzymes. It is possible to determine meaningful thermostability parameters from the routinely acquired data through a straightforward method that is not only more informative but also provides a means to compare thermostability of enzymes from different sources. Here, we describe a simple, effective, and economical way to determine enzyme thermostability. In our opinion, including this method in Biochemistry and Molecular Biology curricula will encourage students to include thermostability analysis in their future work, leading to a more meaningful approach to evaluate and compare enzymes. Furthermore, as the method requires minimum specialized equipment, the analysis will be particularly suitable for labs that cannot afford expensive setup. © 2018 by The International Union of Biochemistry and Molecular Biology, 46:398-402, 2018.

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Isolation and characterization of a 1,4-beta-D-glucan glucohydrolase from the yeast, Torulopsis wickerhamii.

Cited by 17 publications

References 60 publications

Efficient biomass saccharification using a novel cellobiohydrolase from Clostridium clariflavum for utilization in biofuel industry

Efficient biomass saccharification using a novel cellobiohydrolase from Clostridium clariflavum for utilization in biofuel industry

Characterization of a cellodextrin glucohydrolase with soluble oligomeric substrates: Experimental results and modeling of concentration‐time‐course data

How to calculate thermostability of enzymes using a simple approach

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