FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4313442554> ?p ?o ?g. }

• W4313442554 endingPage "102963" @default.
• W4313442554 startingPage "102963" @default.
• W4313442554 abstract "Specific combinations of enzymes depolymerize lignocellulosic biomass into respective monomers following various complex kinetic pathways. Conversion of biomass to biofuel through sugar platform is substantiated with specific kinetics controlling enzymatic hydrolysis in presence of unavoidable inhibitors. Some amount of lignin, still present in the delignified biomass broth acts as a substrate inhibitor for the specific group of cellulolytic enzymes during hydrolysis. Considering state-of-the-art research works, biomass to enzyme ratio is highlighted as one of the key factors in biomass hydrolysis, followed by time and agitation speed. Correlations between various kinetic parameters and different process variables are analysed in-depth using experimental outcomes as well as model predictions. Role of process parameters on hydrolysis outcomes, highlighting specific inhibition kinetics, deactivation of enzymes, and effect of mechanical agitation, is discussed thoroughly. Fractal kinetics and optimum product inhibition are also reviewed on a comparative basis. In order to understand the role of specific oligosaccharides on inhibition, the effects of mobility of sugar molecules, enzymatic trans-glycosylation, modes of hydrolysis (batch or fed-batch) on sugar yield are elaborated with respect to monomeric sugar supplements. Most research works have strong evidences to support that addition of other monosaccharides (excluding the end products) like glucose, galactose, mannose, fructose, of similar concentration, lowers the glucose yield to different degrees. Supplements of monomeric sugars, except xylose, increase the Michaelis-Menten [MM] constant, showing a reduced affinity of enzymes towards the substrate, through the competitive mode of inhibition. Xylose, however, exhibits a non-competitive type inhibition, through a strong affinity for the enzyme, enzyme-substrate, and enzyme-cellobiose complex. Most of the researchers focus on the removal of glucose as a primary end product in order to abate inhibition, except some periodically removed cellobiose. Cellobiohydrolase alone can generate cellobiose much more than endoglucanase alone. The synergistic action of different cellulolytic enzymes is found beneficial in terms of sugar generation. Product inhibition remains a crucial factor that needs to be overcome in order to attain a higher concentration of specific mono sugars." @default.
• W4313442554 created "2023-01-06" @default.
• W4313442554 creator A5014600998 @default.
• W4313442554 creator A5020017690 @default.
• W4313442554 creator A5048365009 @default.
• W4313442554 creator A5089594500 @default.
• W4313442554 creator A5091374848 @default.
• W4313442554 date "2023-02-01" @default.
• W4313442554 modified "2023-10-18" @default.
• W4313442554 title "Conversion of biomass to biofuels through sugar platform: A review of enzymatic hydrolysis highlighting the trade-off between product and substrate inhibitions" @default.
• W4313442554 cites W1508268801 @default.
• W4313442554 cites W1963845880 @default.
• W4313442554 cites W1966860372 @default.
• W4313442554 cites W1969925056 @default.
• W4313442554 cites W1970098118 @default.
• W4313442554 cites W1973020326 @default.
• W4313442554 cites W1973068721 @default.
• W4313442554 cites W1979361554 @default.
• W4313442554 cites W1979834301 @default.
• W4313442554 cites W1984156524 @default.
• W4313442554 cites W1984845518 @default.
• W4313442554 cites W1987200857 @default.
• W4313442554 cites W1990804935 @default.
• W4313442554 cites W1992758631 @default.
• W4313442554 cites W1993940896 @default.
• W4313442554 cites W2004304946 @default.
• W4313442554 cites W2006103512 @default.
• W4313442554 cites W2007575896 @default.
• W4313442554 cites W2008000102 @default.
• W4313442554 cites W2009558977 @default.
• W4313442554 cites W2011381419 @default.
• W4313442554 cites W2031938688 @default.
• W4313442554 cites W2046663612 @default.
• W4313442554 cites W2055760629 @default.
• W4313442554 cites W2058562056 @default.
• W4313442554 cites W2064183259 @default.
• W4313442554 cites W2071446680 @default.
• W4313442554 cites W2072346888 @default.
• W4313442554 cites W2080525098 @default.
• W4313442554 cites W2084704671 @default.
• W4313442554 cites W2092039690 @default.
• W4313442554 cites W2094139824 @default.
• W4313442554 cites W2094215650 @default.
• W4313442554 cites W2097112371 @default.
• W4313442554 cites W2114250357 @default.
• W4313442554 cites W2121527292 @default.
• W4313442554 cites W2154757083 @default.
• W4313442554 cites W2157817705 @default.
• W4313442554 cites W2251725413 @default.
• W4313442554 cites W2277099242 @default.
• W4313442554 cites W2411959437 @default.
• W4313442554 cites W2418142840 @default.
• W4313442554 cites W2481913962 @default.
• W4313442554 cites W2508506265 @default.
• W4313442554 cites W2751544302 @default.
• W4313442554 cites W2756404960 @default.
• W4313442554 cites W2781669628 @default.
• W4313442554 cites W2790442202 @default.
• W4313442554 cites W2798098850 @default.
• W4313442554 cites W2800641504 @default.
• W4313442554 cites W2800676679 @default.
• W4313442554 cites W2809169695 @default.
• W4313442554 cites W2809254964 @default.
• W4313442554 cites W2869873496 @default.
• W4313442554 cites W2879159469 @default.
• W4313442554 cites W2888361599 @default.
• W4313442554 cites W2893831039 @default.
• W4313442554 cites W2896709254 @default.
• W4313442554 cites W2911851509 @default.
• W4313442554 cites W2918365901 @default.
• W4313442554 cites W2940335390 @default.
• W4313442554 cites W2946659613 @default.
• W4313442554 cites W2995604951 @default.
• W4313442554 cites W3001647935 @default.
• W4313442554 cites W3008788754 @default.
• W4313442554 cites W3021685191 @default.
• W4313442554 cites W3022265187 @default.
• W4313442554 cites W3084625281 @default.
• W4313442554 cites W3094156481 @default.
• W4313442554 cites W3094253148 @default.
• W4313442554 cites W3168838301 @default.
• W4313442554 cites W3179835563 @default.
• W4313442554 cites W3184290617 @default.
• W4313442554 cites W3206590724 @default.
• W4313442554 cites W3208411549 @default.
• W4313442554 cites W4247175524 @default.
• W4313442554 cites W655318307 @default.
• W4313442554 doi "https://doi.org/10.1016/j.seta.2022.102963" @default.
• W4313442554 hasPublicationYear "2023" @default.
• W4313442554 type Work @default.
• W4313442554 citedByCount "0" @default.
• W4313442554 crossrefType "journal-article" @default.
• W4313442554 hasAuthorship W4313442554A5014600998 @default.
• W4313442554 hasAuthorship W4313442554A5020017690 @default.
• W4313442554 hasAuthorship W4313442554A5048365009 @default.
• W4313442554 hasAuthorship W4313442554A5089594500 @default.
• W4313442554 hasAuthorship W4313442554A5091374848 @default.
• W4313442554 hasBestOaLocation W43134425541 @default.

• next