Pub Date : 2019-01-30DOI: 10.5772/INTECHOPEN.79848
A. Serafin-Muñoz, C. Molina–Guerrero, B. N. Luna, Julio César Leal Vaca, A. Á. Vargas
The pretreatment of biomass has been integrated with enzyme production through the recycling of aqueous fractions. A process integrated with Pleurotus cystidiosus was grown, and enzymatic hydrolysis was realized. Samples of every liquid fraction from the fungal growing medium were analyzed to determine the chemical oxygen demand (OCD), glucose (Glu), xylose (Xyl), and total reducing sugars (RS). Separately, to obtain valuable polymers from this integration process, solid hemicellulose and lignin were isolated from the remaining liquid fractions through pH variation. The composition of the samples was determined using scanning electron microscopy (SEM), optical stereoscopic microscopy, and Fourier transform infrared (FTIR) spectroscopy and was compared with commercial homologs. The maximum conversion of cellulose to glucose by the obtained liquid fraction of the fungal medium was 61.3 ± 0.9% of the theoretical conversion yield of the commercial enzyme. Similarly, the conversion of hemicelluloses to xylose was 69.5 ± 1.5%. Finally, in this work, an integrated platform for cellulose, hemicellulose, lignin, enzymatic extract, and sugars production, which also significantly reduces water consumption, was proposed. at a of −1 in performed on each
{"title":"Obtaining Enzymatic Extract from Pleurotus spp. Associated with an Integrated Process for Conversion of Lignocellulosic Biomass to Bioproducts","authors":"A. Serafin-Muñoz, C. Molina–Guerrero, B. N. Luna, Julio César Leal Vaca, A. Á. Vargas","doi":"10.5772/INTECHOPEN.79848","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.79848","url":null,"abstract":"The pretreatment of biomass has been integrated with enzyme production through the recycling of aqueous fractions. A process integrated with Pleurotus cystidiosus was grown, and enzymatic hydrolysis was realized. Samples of every liquid fraction from the fungal growing medium were analyzed to determine the chemical oxygen demand (OCD), glucose (Glu), xylose (Xyl), and total reducing sugars (RS). Separately, to obtain valuable polymers from this integration process, solid hemicellulose and lignin were isolated from the remaining liquid fractions through pH variation. The composition of the samples was determined using scanning electron microscopy (SEM), optical stereoscopic microscopy, and Fourier transform infrared (FTIR) spectroscopy and was compared with commercial homologs. The maximum conversion of cellulose to glucose by the obtained liquid fraction of the fungal medium was 61.3 ± 0.9% of the theoretical conversion yield of the commercial enzyme. Similarly, the conversion of hemicelluloses to xylose was 69.5 ± 1.5%. Finally, in this work, an integrated platform for cellulose, hemicellulose, lignin, enzymatic extract, and sugars production, which also significantly reduces water consumption, was proposed. at a of −1 in performed on each","PeriodicalId":136596,"journal":{"name":"Kinetics of Enzymatic Synthesis","volume":"35 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2019-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"121842576","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2018-11-20DOI: 10.5772/INTECHOPEN.81333
N. Azudin, S. R. Shukor
Isoamyl acetate is an organic compound which is mainly used as flavor additive in food industries. Traditionally, the food flavor has been produced by extraction from plants, followed by chemical synthesis route which then shifted to biocatalytic route due to consumer ’ s awareness and inclination toward natural products. This study was carried out to examine the reaction synthesis between acetic anhydride and isoamyl alcohol in the presence of Candida antarctica Lipase-B (CALB) as a catalyst in solvent-free system (SFS). Results show that two reactions took place between acetic anhydride and isoamyl alcohol. The effect of different reaction parameters on the final yield of isoamyl acetate and the optimization of process parameters using a statistical tool were also investigated with response surface methodology (RSM). It was found that the optimum isoamyl acetate yield is at reaction temperature 30 (cid:1) C, acid/alcohol molar ratio 0.10, and enzyme loading 4.14%. The regression coefficient for optimization based on RSM was 0.9961. Errors resulted from model validation is less than 1% and is acceptable for real-life application. RSM model and first principle model were selected to determine the reaction kinetics and yield of reaction for isoamyl acetate. The results showed that RSM model provides a good predication of the esterification system with R 2 value of 0.90.
{"title":"Solvent-Free Isoamyl Acetate Production via Enzymatic Esterification","authors":"N. Azudin, S. R. Shukor","doi":"10.5772/INTECHOPEN.81333","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.81333","url":null,"abstract":"Isoamyl acetate is an organic compound which is mainly used as flavor additive in food industries. Traditionally, the food flavor has been produced by extraction from plants, followed by chemical synthesis route which then shifted to biocatalytic route due to consumer ’ s awareness and inclination toward natural products. This study was carried out to examine the reaction synthesis between acetic anhydride and isoamyl alcohol in the presence of Candida antarctica Lipase-B (CALB) as a catalyst in solvent-free system (SFS). Results show that two reactions took place between acetic anhydride and isoamyl alcohol. The effect of different reaction parameters on the final yield of isoamyl acetate and the optimization of process parameters using a statistical tool were also investigated with response surface methodology (RSM). It was found that the optimum isoamyl acetate yield is at reaction temperature 30 (cid:1) C, acid/alcohol molar ratio 0.10, and enzyme loading 4.14%. The regression coefficient for optimization based on RSM was 0.9961. Errors resulted from model validation is less than 1% and is acceptable for real-life application. RSM model and first principle model were selected to determine the reaction kinetics and yield of reaction for isoamyl acetate. The results showed that RSM model provides a good predication of the esterification system with R 2 value of 0.90.","PeriodicalId":136596,"journal":{"name":"Kinetics of Enzymatic Synthesis","volume":"12 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"127895455","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2018-11-12DOI: 10.5772/INTECHOPEN.80228
Kalim Belhacene, I. Ungureanu, E. Grosu, R. Przybylski, A. Blaga, P. Dhulster, R. Froidevaux
Intensification of process is increasingly interesting in the context of recovery of indus - trial wastes. Among these compounds, animal blood is underexploited although it is an important source of bioactive peptides. LVV-h7 (LVVYPWTQRF) is one of these bioactive peptides from bovine haemoglobin hydrolysate. Our innovative approach consists of a continuous process involving at microfluidic scale for enzymatic proteolysis of bovine haemoglobin by pepsin, selective extraction of LVV-h7 to an organic solvent during the enzymatic reaction, followed by a second extraction to an aqueous phase for organic solvent recycling. Thus, the obtainment of pure LVV-h7 peptide with an efficient meth odology of extraction and solvent recycling was proved.
{"title":"From a Sequential to a Continuous Approach for LVV-h7 Preparation during Enzymatic Proteolysis in a Microfluidic- Based Extraction Process","authors":"Kalim Belhacene, I. Ungureanu, E. Grosu, R. Przybylski, A. Blaga, P. Dhulster, R. Froidevaux","doi":"10.5772/INTECHOPEN.80228","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.80228","url":null,"abstract":"Intensification of process is increasingly interesting in the context of recovery of indus - trial wastes. Among these compounds, animal blood is underexploited although it is an important source of bioactive peptides. LVV-h7 (LVVYPWTQRF) is one of these bioactive peptides from bovine haemoglobin hydrolysate. Our innovative approach consists of a continuous process involving at microfluidic scale for enzymatic proteolysis of bovine haemoglobin by pepsin, selective extraction of LVV-h7 to an organic solvent during the enzymatic reaction, followed by a second extraction to an aqueous phase for organic solvent recycling. Thus, the obtainment of pure LVV-h7 peptide with an efficient meth odology of extraction and solvent recycling was proved.","PeriodicalId":136596,"journal":{"name":"Kinetics of Enzymatic Synthesis","volume":"32 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-11-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"123397005","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2018-11-05DOI: 10.5772/INTECHOPEN.80235
A. Wangler, M. Bunse, G. Sadowski, C. Held
The classical approach towards analysing the influence of co-solvents (i.e., cellular mole- cules that are chemically inert and do not act as reacting agents) on the Michaelis constants of enzyme-catalysed reactions is empirical. More precisely, reaction kinetics is usually mathematically modelled by fitting empirical parameters to experimental concentration vs. time data. In this chapter, a thermodynamic approach is presented that replaces substrate concentrations by thermodynamic activities of the substrates. This approach allows determining activity-based Michaelis constants. The advantage of such activity-based constants K aM over their concentration-based pendants K obsM is twofold: First, K aM is independent of any co-solvent added (while K obsM is not) as long as it does not directly interfere with the reaction mechanism (e.g., inhibitor or activator). Second, known K aM values allow predictions of Michalis constants for different enzymes and reactions under co-solvent influence. This is demonstrated for a pseudo-one-substrate peptide hydrolysis reaction as well as for more complex two-substrate alcohol dehydrogenase reactions.
{"title":"Thermodynamic Activity-Based Michaelis Constants","authors":"A. Wangler, M. Bunse, G. Sadowski, C. Held","doi":"10.5772/INTECHOPEN.80235","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.80235","url":null,"abstract":"The classical approach towards analysing the influence of co-solvents (i.e., cellular mole- cules that are chemically inert and do not act as reacting agents) on the Michaelis constants of enzyme-catalysed reactions is empirical. More precisely, reaction kinetics is usually mathematically modelled by fitting empirical parameters to experimental concentration vs. time data. In this chapter, a thermodynamic approach is presented that replaces substrate concentrations by thermodynamic activities of the substrates. This approach allows determining activity-based Michaelis constants. The advantage of such activity-based constants K aM over their concentration-based pendants K obsM is twofold: First, K aM is independent of any co-solvent added (while K obsM is not) as long as it does not directly interfere with the reaction mechanism (e.g., inhibitor or activator). Second, known K aM values allow predictions of Michalis constants for different enzymes and reactions under co-solvent influence. This is demonstrated for a pseudo-one-substrate peptide hydrolysis reaction as well as for more complex two-substrate alcohol dehydrogenase reactions.","PeriodicalId":136596,"journal":{"name":"Kinetics of Enzymatic Synthesis","volume":"112 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"128105133","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2018-11-05DOI: 10.5772/INTECHOPEN.81100
L. A. Cira-Chávez, Joseph Guevara-Luna, Marisela YadiraSoto-Padilla, Brenda Román-Ponce, M. Vásquez-Murrieta, M. I. Estrada-Alvarado
Hypersaline environments are those with salt concentrations 9–10 times higher (30–35% of NaCl) than sea water (3.5% of NaCl). At high concentrations of soluble salts, cytoplasm—mainly of bacteria and archaea—is exposed to high ionic strength and achieves osmotic equilibrium by maintaining a cytoplasmic salt concentration similar to that of the surrounding media. Halophilic enzymes are extremozymes produced by halophilic microorganisms; they have similar characteristics to regular enzymes but different prop -erties, mainly structural. Among these properties is a high requirement of salt for biologi- cal functions. Furthermore, the discovery of enzymes capable of degrading biopolymers offer a new perspective in the treatment of residues from oil deposits, under typically high conditions of salt and temperature, while giving valuable information on heterotrophic processes in saline environments.
{"title":"Kinetics of Halophilic Enzymes","authors":"L. A. Cira-Chávez, Joseph Guevara-Luna, Marisela YadiraSoto-Padilla, Brenda Román-Ponce, M. Vásquez-Murrieta, M. I. Estrada-Alvarado","doi":"10.5772/INTECHOPEN.81100","DOIUrl":"https://doi.org/10.5772/INTECHOPEN.81100","url":null,"abstract":"Hypersaline environments are those with salt concentrations 9–10 times higher (30–35% of NaCl) than sea water (3.5% of NaCl). At high concentrations of soluble salts, cytoplasm—mainly of bacteria and archaea—is exposed to high ionic strength and achieves osmotic equilibrium by maintaining a cytoplasmic salt concentration similar to that of the surrounding media. Halophilic enzymes are extremozymes produced by halophilic microorganisms; they have similar characteristics to regular enzymes but different prop -erties, mainly structural. Among these properties is a high requirement of salt for biologi- cal functions. Furthermore, the discovery of enzymes capable of degrading biopolymers offer a new perspective in the treatment of residues from oil deposits, under typically high conditions of salt and temperature, while giving valuable information on heterotrophic processes in saline environments.","PeriodicalId":136596,"journal":{"name":"Kinetics of Enzymatic Synthesis","volume":"1 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2018-11-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"122664342","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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