Enzymatic hydrolysis of high-moisture corn fiber pretreated by afex and recovery and recycling of the enzyme complex

1997 ◽  
Vol 67 (1-2) ◽  
pp. 113-126 ◽  
Author(s):  
M. Moniruzzaman ◽  
B. E. Dale ◽  
R. B. Hespell ◽  
R. J. Bothast
1963 ◽  
Vol 41 (1) ◽  
pp. 719-730 ◽  
Author(s):  
Paul J. Fritz ◽  
Paul Melius

A new preparation of hog pancreatic lipase is described which is evidently the most stable one of its kind. From the composition of the reaction mixtures after enzymatic hydrolysis with and without sodium taurocholate, it appears that the hydrolysis of triglyceride to diglyceride is facilitated and the hydrolysis of diglyceride to monoglyceride is depressed in the presence of taurocholate. The differences in the curves showing the rates of hydrolysis of triolein, monoolein, tributyrin, and monobutyrin in the presence and absence of taurocholate also indicate that the taurocholate acts to split the diglyceride–enzyme complex and thus increases the action of the enzyme on the triglyceride ester. The hydrolysis of the triglyceride is a fast reaction whereas the di- and mono-glycerides are hydrolyzed at much slower rates. The activation energy for the lipolysis of the triolein and tributyrin has been calculated in the presence and absence of taurocholate. This was possible because in spite of earlier reports that the lipolysis of triolein was not temperature dependent between 10 and 40 degrees, we found these reactions to be temperature dependent. The lesser activating effect at the highest taurocholate concentrations indicates this is not a simple emulsifying effect.


1963 ◽  
Vol 41 (3) ◽  
pp. 719-730 ◽  
Author(s):  
Paul J. Fritz ◽  
Paul Melius

A new preparation of hog pancreatic lipase is described which is evidently the most stable one of its kind. From the composition of the reaction mixtures after enzymatic hydrolysis with and without sodium taurocholate, it appears that the hydrolysis of triglyceride to diglyceride is facilitated and the hydrolysis of diglyceride to monoglyceride is depressed in the presence of taurocholate. The differences in the curves showing the rates of hydrolysis of triolein, monoolein, tributyrin, and monobutyrin in the presence and absence of taurocholate also indicate that the taurocholate acts to split the diglyceride–enzyme complex and thus increases the action of the enzyme on the triglyceride ester. The hydrolysis of the triglyceride is a fast reaction whereas the di- and mono-glycerides are hydrolyzed at much slower rates. The activation energy for the lipolysis of the triolein and tributyrin has been calculated in the presence and absence of taurocholate. This was possible because in spite of earlier reports that the lipolysis of triolein was not temperature dependent between 10 and 40 degrees, we found these reactions to be temperature dependent. The lesser activating effect at the highest taurocholate concentrations indicates this is not a simple emulsifying effect.


Author(s):  
Marcin Lukasiewicz ◽  
Anna Osowiec ◽  
Magdalena Marciniak

2018 ◽  
Author(s):  
Ángel Batallas ◽  
Erenio González ◽  
Carmen Salvador ◽  
Jonathan Villavicencio ◽  
Humberto González Gavilánez ◽  
...  

2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai

Background: Enzymatic hydrolysis of cellulose is an expensive approach due to the high cost of an enzyme involved in the process. The goal of the current study was to apply magnetic nanomaterials as a support for immobilization of enzyme, which helps in the repeated use of immobilized enzyme for hydrolysis to make the process cost-effective. In addition, it will also provide stability to enzyme and increase its catalytic activity. Objective: The main aim of the present study is to immobilize cellulase enzyme on Magnetic Nanoparticles (MNPs) in order to enable the enzyme to be re-used for clean sugar production from cellulose. Methods: MNPs were synthesized using chemical precipitation methods and characterized by different techniques. Further, cellulase enzyme was immobilized on MNPs and efficacy of free and immobilized cellulase for hydrolysis of cellulose was evaluated. Results: Enzymatic hydrolysis of cellulose by immobilized enzyme showed enhanced catalytic activity after 48 hours compared to free enzyme. In first cycle of hydrolysis, immobilized enzyme hydrolyzed the cellulose and produced 19.5 ± 0.15 gm/L of glucose after 48 hours. On the contrary, free enzyme produced only 13.7 ± 0.25 gm/L of glucose in 48 hours. Immobilized enzyme maintained its stability and produced 6.15 ± 0.15 and 3.03 ± 0.25 gm/L of glucose in second and third cycle, respectively after 48 hours. Conclusion: This study will be very useful for sugar production because of enzyme binding efficiency and admirable reusability of immobilized enzyme, which leads to the significant increase in production of sugar from cellulosic materials.


2020 ◽  
Vol 204 ◽  
pp. 106407 ◽  
Author(s):  
Shengxin An ◽  
Wenzhi Li ◽  
Fengyang Xue ◽  
Xu Li ◽  
Ying Xia ◽  
...  

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