The largest database of trusted experimental protocols

87h column

Manufactured by Bio-Rad
Sourced in United States

The 87H column is a chromatography column used for the separation and purification of biomolecules. It is designed for efficient ion exchange and size exclusion chromatography. The column's core function is to facilitate the separation and isolation of target molecules from complex mixtures.

Automatically generated - may contain errors

6 protocols using 87h column

1

Enzymatic Hydrolysis of Pretreated Hardwoods

Check if the same lab product or an alternative is used in the 5 most similar protocols

Example 37

To assess the effect of various enzymes on pretreated mixed hardwoods (PHW), an assay was conducted with 2% solids, pH 5.0 and 38° C. Yeast-produced and purified enzymes were assessed in the assay either with or without additional commercial enzymes. The activity of the mix with yeast-produced enzymes evaluated by the release of sugars, predominantly glucose due to the nature of the pretreatment, by HPLC using a BioRad 87H column. The data below shows the results of some of those mixing experiments. FIG. 94 shows that the addition of CBH2, BGL, EG1, EG2 and EG3 improves hydrolysis of the substrate above what the commercial enzyme mix can do with just the addition of CBH2 and BGL. Therefore, yeast-made EG1, EG2 and EG3 provide benefits in hydrolyzing PHW. FIG. 95 shows that further addition of yeast-produced and purified xylanase, xylosidase and AXE improved hydrolysis of the PHW above what was seen with either just the commercial enzyme mix or the commercial mix with CBH2 added. This further suggests the benefits of the accessory enzymes described above.

FIG. 96 shows that the addition of these enzymes in combination continues to show improvement over the addition of just one of the accessory enzymes.

+ Open protocol
+ Expand
2

Enzymatic Hydrolysis of Pretreated Hardwoods

Check if the same lab product or an alternative is used in the 5 most similar protocols

Example 37

To assess the effect of various enzymes on pretreated mixed hardwoods (PHW), an assay was conducted with 2% solids, pH 5.0 and 38° C. Yeast-produced and purified enzymes were assessed in the assay either with or without additional commercial enzymes. The activity of the mix with yeast-produced enzymes evaluated by the release of sugars, predominantly glucose due to the nature of the pretreatment, by HPLC using a BioRad 87H column. The data below shows the results of some of those mixing experiments. FIG. 94 shows that the addition of CBH2, BGL, EG1, EG2 and EG3 improves hydrolysis of the substrate above what the commercial enzyme mix can do with just the addition of CBH2 and BGL. Therefore, yeast-made EG1, EG2 and EG3 provide benefits in hydrolyzing PHW. FIG. 95 shows that further addition of yeast-produced and purified xylanase, xylosidase and AXE improved hydrolysis of the PHW above what was seen with either just the commercial enzyme mix or the commercial mix with CBH2 added. This further suggests the benefits of the accessory enzymes described above.

FIG. 96 shows that the addition of these enzymes in combination continues to show improvement over the addition of just one of the accessory enzymes.

+ Open protocol
+ Expand
3

HPLC Analysis of Fermentation Acids

Check if the same lab product or an alternative is used in the 5 most similar protocols
The contents of acetic acid and lactic acid in the fermentation culture were determined using high performance liquid chromatography (HPLC) with refractive index detector (RID). A Bio-Rad 87H column (Bio-Rad, Hercules, CA, USA) was used and eluted with 5 mM H2SO4 as a mobile phase at column temperature of 60 °C and a flow rate of 0.6 mL/min.
+ Open protocol
+ Expand
4

Biomass and Electrochemical Characterization of MFCs

Check if the same lab product or an alternative is used in the 5 most similar protocols
The biomass of the electricity generation process was determined by measuring the absorbance values of the samples at 600 nm using a UV spectrophotometer (OnLab, China, Shanghai). An LC20-AT high-performance liquid chromatograph (Shimadzu, Japan) was used to detect the concentration of glucose and ethanol in the anode electrolyte. A BIO-Rad 87H column was used with 5 mM sulfuric acid as the mobile phase, a column temperature of 65 °C, a flow rate of 0.6 ml/min, an injection volume of 10 μL, and a detector with an oscillometric detector. Intracellular NAD(P)+ and NAD(P)H were analyzed using NADH/ NAD+ and NADPH/ NADP+ quantification kit (Suzhou Comin Biotechnology Co., Ltd., USA). The open-circuit potential and external-circuit potential of the MFC were measured using a potentiostat (CHI660E, Chenhua Co., Ltd., China, Shanghai). The polarization curves were obtained using linear scanning voltammetry with a sweep rate of 2 mV/s. Cyclic voltammetry and electrochemical impedance spectroscopy (EIS) were conducted using a three-electrode system with Ag/AgCl as the reference electrode and a cyclic voltammetry scan rate of 1 mV/s. EIS were conducted over a frequency range of 0.01 Hz to 100 kHz at open circuit potential, with a perturbation signal of 10 mV. Nyquist plots were simulated as an equivalent circuit (Additional file 1: Fig. S9) using a fitting program (ZsimpWin 3.10).
+ Open protocol
+ Expand
5

Optimizing Lignocellulosic Biomass Hydrolysis

Check if the same lab product or an alternative is used in the 5 most similar protocols

Example 37

To assess the effect of various enzymes on pretreated mixed hardwoods (PHW), an assay was conducted with 2% solids, pH 5.0 and 38° C. Yeast-produced and purified enzymes were assessed in the assay either with or without additional commercial enzymes. The activity of the mix with yeast-produced enzymes evaluated by the release of sugars, predominantly glucose due to the nature of the pretreatment, by HPLC using a BioRad 87H column. The data below shows the results of some of those mixing experiments. FIG. 94 shows that the addition of CBH2, BGL, EG1, EG2 and EG3 improves hydrolysis of the substrate above what the commercial enzyme mix can do with just the addition of CBH2 and BGL. Therefore, yeast-made EG1, EG2 and EG3 provide benefits in hydrolyzing PHW. FIG. 95 shows that further addition of yeast-produced and purified xylanase, xylosidase and AXE improved hydrolysis of the PHW above what was seen with either just the commercial enzyme mix or the commercial mix with CBH2 added. This further suggests the benefits of the accessory enzymes described above.

FIG. 96 shows that the addition of these enzymes in combination continues to show improvement over the addition of just one of the accessory enzymes.

+ Open protocol
+ Expand
6

Enzymatic Hydrolysis of Pretreated Hardwood

Check if the same lab product or an alternative is used in the 5 most similar protocols
To determine the accessibility of the substrate to enzymatic attack, a hydrolysis experiment was done in which a dose curve of commercially available enzyme, Flashzyme from AB Enzymes, was added to 2.5 % substrate (either pretreated or chlorite extracted pretreated hardwood) diluted in 50 mM sodium citrate buffer, pH 5.2. The plate was incubated at 35 °C while stirring and sampled daily for carbohydrate analysis by HPLC on a BioRad 87H column as described in (method below). The amount of sugar released enzymatically was compared to the values obtained by quantitative saccharification to determine the extent of hydrolysis.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!