Pretreatment and enzymatic saccharification of oak at high solids loadings to obtain high titers and high yields of sugars

2019 ◽  
Vol 284 ◽  
pp. 391-397 ◽  
Author(s):  
Dong Hyun Kim ◽  
Hyun Min Park ◽  
Young Hoon Jung ◽  
Prakit Sukyai ◽  
Kyoung Heon Kim
Keyword(s):  
Enzymatic Saccharification ◽  
High Solids ◽  
High Yields

Fed-Batch Enzymatic Saccharification of High Solids Pretreated Lignocellulose for Obtaining High Titers and High Yields of Glucose

2017 ◽  
Vol 182 (3) ◽  
pp. 1108-1120 ◽  
Author(s):  
Young Hoon Jung ◽  
Hyun Min Park ◽  
Dong Hyun Kim ◽  
Jungwoo Yang ◽  
Kyoung Heon Kim
Keyword(s):  
Enzymatic Saccharification ◽  
High Solids ◽  
Fed Batch ◽  
High Yields

A New Multiple-Dilution-Assays Method for Determining Glucose Yield from Enzymatic Saccharification of Biomass at High-Solids Loadings

2019 ◽  
Vol 15 (6) ◽  
pp. 685-693
Author(s):  
Han Zhang ◽  
Hao Liu ◽  
Jianliang Sun ◽  
Mingqian Mai ◽  
Shiyu Fu ◽  
...  
Keyword(s):  
Enzymatic Saccharification ◽  
High Accuracy ◽  
Liquid Volume ◽  
Liquid Density ◽  
High Solids ◽  
Fed Batch ◽  
Glucose Yield ◽  
Biomass Saccharification ◽  
High Level

Background: Determination of the accurate mass of glucose generated from high-solids biomass saccharification is vital but problematic due to the uncertainty of liquid volume and slurry density. Methods: Herein, a new multiple-dilution-assays method was established to deduce the accurate glucose mass from the hydrolyzing biomass slurry. Results: This method was applicable for slurries of pretreated corn stover with a solids consistency up to 30 wt%, showing a high accuracy and good reproducibility. Dryness did not interfere with the accuracy. Ethanol at a high level, e.g. 10%, caused only a small negative error (<2%). This method can be used in either single- or fed-batch high-solids biomass saccharification, allowing to quantify the maldistribution of glucose in the slurry. Conclusion: The significant advantage of the present method was that only one single variable, glucose concentration, was to be determined, rendering it unnecessary to wash the insoluble or to measure the changing liquid density.

Fed-batch high-solids enzymatic saccharification of lignocellulosic substrates with a combination of additives and accessory enzymes

2020 ◽  
Vol 146 ◽  
pp. 112156 ◽  
Author(s):  
Marie Rose Mukasekuru ◽  
Pascal Kaneza ◽  
Haiyan Sun ◽  
Fubao Fuelbiol Sun ◽  
Jing He ◽  
...  
Keyword(s):  
Enzymatic Saccharification ◽  
High Solids ◽  
Fed Batch ◽  
Lignocellulosic Substrates

A Simple Method for Preparing Fibrinogen

1966 ◽  
Vol 16 (01/02) ◽  
pp. 198-206 ◽  
Author(s):  
W Straughn ◽  
R. H Wagner
Keyword(s):  
Barium Sulfate ◽  
Caproic Acid ◽  
Aminobutyric Acid ◽  
Gamma Aminobutyric Acid ◽  
Human Fibrinogen ◽  
Simple Method ◽  
High Yields ◽  
Marked Stability

SummaryA simple new procedure is reported for the isolation of canine, bovine, porcine, and human fibrinogen. Two molar β-alanine is used to precipitate fibrinogen from barium sulfate adsorbed plasma. The procedure is characterized by dependability and high yields. The material is 95% to 98% clottable protein but still contains impurities such as plasminogen and fibrin-stabilizing factor. Plasminogen may be removed by adsorption with charcoal. The fibrinogen preparations exhibit marked stability to freezing, lyophilization, and dialysis. Epsilon-amino-n-caproic acid and gamma-aminobutyric acid which were also studied have the property of precipitating proteins from plasma but lack the specificity for fibrinogen found with β-alanine.

A Novel Method for the Rapid Purification of Human and Rat Fibrin(OGEN) Degradation Products in High Yields

1979 ◽  
Author(s):  
W. Nieuwenhuizen ◽  
I. A. M. van Ruijven-Vermeer ◽  
F. Haverkate ◽  
G. Timan
Keyword(s):  
Degradation Products ◽  
Complete Separation ◽  
Purification Method ◽  
Amino Terminal ◽  
Novel Method ◽  
Rapid Purification ◽  
The One ◽  
High Yields ◽  
Size Heterogeneity ◽  
D Dimer

A novel method will be described for the preparation and purification of fibrin(ogen) degradation products in high yields. The high yields are due to two factors. on the one hand an improved preparation method in which the size heterogeneity of the degradation products D is strongly reduced by plasmin digestion at well-controlled calcium concentrations. At calcium concentrations of 2mM exclusively D fragments, M.W.= 93-000 (Dcate) were formed; in the presence of 1OmM EGTA only fragments M.W.= 80.000 (D EGTA) were formed as described. on the other hand a new purification method, which includes Sephadex G-200 filtration to purify the D:E complexes and separation of the D and E fragments by a 16 hrs. preparative isoelectric focussing. The latter step gives a complete separation of D (fragments) (pH = 6.5) and E fragments (at pH = 4.5) without any overlap, thus allowing a nearly 100% recovery in this step. The overall recoveries are around 75% of the theoretical values. These recoveries are superior to those of existing procedures. Moreover the conditions of this purification procedure are very mild and probably do not affect the native configuration of the products. Amino-terminal amino acids of human Dcate, D EGTA and D-dimer are identical i.e. val, asx and ser. in the ratgly, asx and ser were found. E 1% for rat Dcate=17-8 for rat D EGTA=16.2 and for rat D- dimer=l8.3. for the corresponding human fragments, these values were all 20.0 ± 0.2.

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