Evaluation of the enzymatic susceptibility of cellulosic substrates using specific hydrolysis rates and enzyme adsorption

1994 ◽  
Vol 45-46 (1) ◽  
pp. 407-415 ◽  
Author(s):  
Dora Lee ◽  
Alex H. C. Yu ◽  
Ken K. Y. Wong ◽  
John N. Saddler
Keyword(s):  
Enzyme Adsorption ◽  
Hydrolysis Rates

Environmentally Friendly Preparation of Magnetic Composites Featuring Proteolytic Properties

INEOS OPEN ◽  
2020 ◽  
Author(s):  
N. A. Samoilova ◽  
Keyword(s):  
Enzyme Immobilization ◽  
Maleic Acid ◽  
Environmentally Friendly ◽  
Synthetic Polymer ◽  
Magnetic Composites ◽  
Interpolyelectrolyte Complex ◽  
Hydrolysis Rates ◽  
Poly Ethylene ◽  
Noncovalent Binding

The enzyme-containing magnetic composites are presented. The magnetic matrix for enzyme immobilization is obtained by sequential application of an amine-containing polysaccharide—chitosan and a synthetic polymer—poly(ethylene-alt-maleic acid) to the magnetite microparticles to form the interpolyelectrolyte complex shell. Then, the enzyme (trypsin) is immobilized by covalent or noncovalent binding. Thus, the suggested composites can be readily obtained in the environmentally friendly manner. The enzyme capacity of the resulting composites reaches 28.0–32.6 mg/g. The maximum hydrolysis rates of the H-Val-Leu-Lys-pNA substrate provided by these composites range within 0.60·10–7–0.77·10–7 M/min.

n → π* Interactions in N-Acyl Homoserine Lactone Derivatives and Their Effects on Hydrolysis Rates

2019 ◽  
Vol 123 (13) ◽  
pp. 2537-2543 ◽  
Author(s):  
Daniel J. Schmucker ◽  
Sydney R. Dunbar ◽  
Tricia D. Shepherd ◽  
Michael A. Bertucci
Keyword(s):  
Homoserine Lactone ◽  
Acyl Homoserine Lactone ◽  
Π Interactions ◽  
Hydrolysis Rates

scholarly journals A Novel Thermostable GH3β-Glucosidase fromTalaromyce leycettanuswith Broad Substrate Specificity and Significant Soybean Isoflavone Glycosides-Hydrolyzing Capability

2018 ◽  
Vol 2018 ◽  
pp. 1-9
Author(s):  
Xinxin Li ◽  
Wei Xia ◽  
Yingguo Bai ◽  
Rui Ma ◽  
Hong Yang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glycoside Hydrolase ◽  
Animal Feed ◽  
Amino Acid Residues ◽  
Calculated Molecular Mass ◽  
Substrate Specificities ◽  
Soybean Isoflavone ◽  
Food Animal ◽  
Isoflavone Glycoside ◽  
Hydrolysis Rates

A novelβ-glucosidase gene (Bgl3B) of glycoside hydrolase (GH) family 3 was cloned from the thermophilic fungusTalaromyce leycettanusJM12802 and successfully expressed inPichia pastoris. The deduced Bgl3B contains 860 amino acid residues with a calculated molecular mass of 91.2 kDa. The purified recombinant Bgl3B exhibited maximum activities at pH 4.5 and 65°C and remained stable at temperatures up to 60°C and pH 3.0−9.0, respectively. The enzyme exhibited broad substrate specificities, showingβ-glucosidase, glucanase, cellobiase, xylanase, and isoflavone glycoside hydrolase activities, and its activities were stimulated by short-chain alcohols. The catalytic efficiencies of Bgl3B were 693 and 104/mM/s towardspNPG and cellobiose, respectively. Moreover, Bgl3B was highly effective in converting isoflavone glycosides to aglycones at 37°C within 10 min, with the hydrolysis rates of 95.1%, 76.0%, and 75.3% for daidzin, genistin, and glycitin, respectively. These superior properties make Bgl3B potential for applications in the food, animal feed, and biofuel industries.

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