Click here to see the Celignis Analysis Packages that determine Cellulose Content
Request a QuoteCellulose Content
Click here to see the Celignis Analysis Packages that determine Hemicellulose Content
Request a QuoteHemicellulose Content
Click here to see the Celignis Analysis Packages that determine Lignin Content
Request a QuoteLignin Content
Click here to see the Celignis Analysis Packages that determine Starch Content
Request a QuoteStarch Content
Click here to see the Celignis Analysis Packages that determine Uronic Acid Content
Request a QuoteUronic Acid Content
Click here to see the Celignis Analysis Packages that determine Enzymatic Hydrolysis
Request a QuoteEnzymatic Hydrolysis
Click here to see the Celignis Analysis Packages that determine Ash Content
Request a QuoteAsh Content
Click here to see the Celignis Analysis Packages that determine Heating (Calorific) Value
Request a QuoteHeating (Calorific) Value
Ash Shrinkage Starting Temperature (SST) - This occurs when the area of the test piece of Compost ash falls below 95% of the original test piece area.
Ash Deformation Temperature (DT) - The temperature at which the first signs of rounding of the edges of the test piece occurs due to melting.
Ash Hemisphere Temperature (HT) - When the test piece of Compost ash forms a hemisphere (i.e. the height becomes equal to half the base diameter).
Ash Flow Temperature (FT) - The temperature at which the Compost ash is spread out over the supporting tile in a layer, the height of which is half of the test piece at the hemisphere temperature.
Click here to see the Celignis Analysis Packages that determine Ash Melting Behaviour
Request a QuoteAsh Melting Behaviour
Click here to see the Celignis Analysis Packages that determine Major and Minor Elements
Request a QuoteMajor and Minor Elements
At Celignis we can provide you with crucial data on feedstock suitability for AD as well as on the composition of process residues. For example, we can determine the biomethane potential (BMP) of Compost. The BMP can be considered to be the experimental theoretical maximum amount of methane produced from a feedstock. We moniotor the volume of biogas produced allowing for a cumulative plot over time, accessed via the Celignis Database. Our BMP packages also involve routine analysis of biogas composition (biomethane, carbon dioxide, hydrogen sulphide, ammonia, oxygen). We also provide detailed analysis of the digestate, the residue that remains after a sample has been digested. Our expertise in lignocellulosic analysis can allow for detailed insight regarding the fate of the different biogenic polymers during digestion.
Click here to see the Celignis Analysis Packages that determine BMP
Request a QuoteBMP
At Celignis we can determine the bulk density of biomass samples, including Compost, according to ISO standard 17828 (2015). This method requires the biomass to be in an appropriate form (chips or powder) for density determination.
Click here to see the Celignis Analysis Packages that determine Bulk Density
Request a QuoteBulk Density
Our lab is equipped with a Retsch AS 400 sieve shaker. It can accommodate sieves of up to 40 cm diameter, corresponding to a surface area of 1256 square centimetres. This allows us to determine the particle size distribution of a range of samples, including Compost, by following European Standard methods EN 15149- 1:2010 and EN 15149-2:2010.
Click here to see the Celignis Analysis Packages that determine Particle Size
Request a QuoteParticle Size
The Maximum Protease Activity Was Obtained From P. Aeruginosa MCM B-327 With Soybean Meal 1%, Tryptone 1%, Initial Medium PH 7, Agitation Rate 250 Rpm, Aeration Rate 0.75 Vvm And Fermentation Temperature 30 °C, Under Submerged Fermentation Conditions (SmF). The Protease Productivity At 10 And 120L Fermenters Was Found To Be 16,021 And 9,975 UL-1h-1 Respectively. Kinetics Of Cell Growth Revealed That Specific Cell Growth Rate Was 0.025 H-1. Protease Was Active And Stable At Different PH, Temperatures, In Anionic, Cationic And Non-Ionic Detergent Additives, As Well As In Commercial Detergents. The Protease Exhibited Blood Stains Removing Performance Indicating Its Potential In Detergent Industry. The Dried Ammonium Sulphate Precipitated Protease Was Stable At Room Temperature For A Period Of One Year. The Protease Has Shown Properties Suitable For Its Application In Detergents. The Results Contribute To Basic Knowledge And Application Of Protease From P.Aeruginosa To Detergent Industry. The Studies Will Help To Optimize The Production Of This Protease For Biotechnological Applications. |
Response surface methodological (RSM) optimization of protease by Pseudomonas aeruginosa MCM B327, increased 1.3-fold activity with 1% inoculum having cell density of 27.57 x 109 cells mL-1 at pH 7, 300C and 72 h of incubation. Protease enzyme recovered from P. aeruginosa showed characteristic activities against diverse proteins of hide. Enzyme was found to be active with substrates e.g. casein, Bovine serum albumin, gelatin, elastin, haemoglobin but inactive against keratin and collagen. During leather manufacturing, non-collagenase and non-keratinase activities have advantageous in a quality leather and hair saving process, respectively. Increased proteolytic enzyme concentration (0.1-0.5%) in soaking process showed increased water penetration because of hydrolysis of albumin and elastin proteins as indicated by opened fibers in histopathological sections. These findings suggest, protease secreted by P. aeruginosa may have application in soaking operation of leather processing for minimizing harmful deharing chemicals and processing time. |
The processing of lignocellulosic materials in modern biorefineries will allow for the
production of transport fuels and platform chemicals that could replace petroleum-derived
products. However, there is a critical lack of relevant detailed compositional information
regarding feedstocks relevant to Ireland and Irish conditions. This research has involved the
collection, preparation, and the analysis, with a high level of precision and accuracy, of a
large number of biomass samples from the waste and agricultural sectors. Not all of the
waste materials analysed are considered suitable for biorefining; for example the total sugar
contents of spent mushroom composts are too low. However, the waste paper/cardboard
that is currently exported from Ireland has a chemical composition that could result in high
biorefinery yields and so could make a significant contribution to Ireland’s biofuel demands. |
The focus of this study was on production, purification and characterization of dehairing protease from Pseudomonas aeruginosa MCM B-327, isolated from vermicompost pit soil. Optimum protease activity, 395 U mL?1, was observed in the medium containing soybean meal and tryptone, at pH 7 and 30°C. The crude enzyme exhibited dehairing activity. As compared to chemical method, enzymatic method of dehairing showed reduction in COD, TDS and TSS by 34.28%, 37.32% and 51.58%, respectively. Zymogram of crude enzyme on native-PAGE presented two bands with protease activity of molecular weights of 56 and 67 kDa. Both proteases showed dehairing activity. Out of these, 56 kDa protease (PA02) was purified 3.05-folds with 2.71% recovery. The enzyme was active in pH range 7–9 and temperature 20–50°C with optimum pH of 8 and temperature 35°C. Moreover, the enzyme activity of PA02 protease was not strongly inhibited by specific inhibitor showing the novel nature of enzyme compared to serine, cysteine, aspartyl and metalloproteases. Kinetic studies indicated that substrate specificity of PA02 protease was towards various natural and synthetic proteolytic substrates but inactive against collagen and keratin. These findings suggest protease secreted by P. aeruginosa MCM B-327 may have application in dehairing for environment-friendly leather processing. |
The present invention relates to an extracellular enzyme protease obtained by growing the culture of Pseudomonas aeruginosa MCM B-327 isolated from vermiculture pit soil and deposited in MTCC, IMTECH, Chandigarh with designation MTCC 5270, in production medium of pH 7.0; containing soybean meal and tryptone as raw materials, at 30° C. for 72 h. The organism was also able to produce protease using different agricultural products/byproducts as protein sources. The partially purified non-collagenolytic, calcium independent protease with molecular weight 60 kDa has activity in pH range of 6.0-11.0 and temperature range of 25-65° C.; stability in pH range of 6.0-10.0 and temperature 25-45° C. The protease activity was retained for 8 months when stored at ambient temperature. Ammonium sulphate precipitated enzyme was able to completely dehair animal skins and hides without chemicals like lime, sodium sulphide and calcium. |
The present invention relates to an extracellular enzyme protease obtained by growing the culture of Pseudomonas aeruginosa MCM B-327 isolated from vermiculture pit soil and deposited in MTCC, IMTECH, Chandigarh with designation MTCC 5270, in production medium of pH 7.0; containing soybean meal and tryptone as raw materials, at 30° C. for 72 h. The organism was also able to produce protease using different agricultural products/byproducts as protein sources. The partially purified non-collagenolytic, calcium independent protease with molecular weight 60 kDa has activity in pH range of 6.0-11.0 and temperature range of 25-65° C.; stability in pH range of 6.0-10.0 and temperature 25-45° C. The protease activity was retained for 8 months when stored at ambient temperature. Ammonium sulphate precipitated enzyme was able to completely dehair animal skins and hides without chemicals like lime, sodium sulphide and calcium. |
The present invention relates to an extracellular enzyme protease obtained by growing the culture of Pseudomonas aeruginosa MCM B-327 isolated from vermiculture pit soil and deposited in MTCC, IMTECH, Chandigarh with designation MTCC 5270, in production medium of pH 7.0; containing soybean meal and tryptone as raw materials, at 30° C. for 72 h. The organism was also able to produce protease using different agricultural products/byproducts as protein sources. The partially purified non-collagenolytic, calcium independent protease with molecular weight 60 kDa has activity in pH range of 6.0-11.0 and temperature range of 25-65° C.; stability in pH range of 6.0-10.0 and temperature 25-45° C. The protease activity was retained for 8 months when stored at ambient temperature. Ammonium sulphate precipitated enzyme was able to completely dehair animal skins and hides without chemicals like lime, sodium sulphide and calcium. |