Hidrólisis enzimática de residuos de la cosecha de caña de azúcar

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Bibliographic Details
Main Authors: Jairo G. Salcedo Mendoza, Jorge E. Galán López, Luz Marina Pardo Flórez
Format: Article
Language:Spanish
Published: Universidad Nacional de Colombia 2012-04-01
Series:Revista Colombiana de Biotecnología
Subjects:
Online Access:http://www.revistas.unal.edu.co/index.php/biotecnologia/article/view/32797
Description
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La hidrólisis se llevó a cabo a un pH de 4.2 y una temperatura de 50 <sup>o</sup>C. Fueron analizados <span style="mso-spacerun: yes;"> </span>modelos de inhibición por sustrato, glucosa e inhibición total por producto. Los resultados mostraron que los modelos que mejor se ajustan a los datos experimentales, son los modelos de inhibición competitiva por glucosa, con una constante de Michaelis (K<sub>m</sub>) de 20.37 g/L, <span style="mso-spacerun: yes;"> </span>velocidad máxima (V<sub>max</sub>) 39 g/L h y una constante de inhibición<span style="mso-spacerun: yes;">  </span>(k<sub>i</sub>) de 0.442. En el caso que las relaciones <span style="mso-spacerun: yes;"> </span>enzima – Sustrato (E/S) sean mayores<span style="mso-spacerun: yes;">  </span>de 0.5, se puede aplicar el modelo cinético de Michaelis-Menten.</span></p> <p class="MsoNormal" style="margin-bottom: .0001pt; text-align: justify; line-height: normal;"><strong style="mso-bidi-font-weight: normal;"><span style="font-size: 10.0pt; font-family: ">Palabras clave</span></strong><span style="font-size: 10.0pt; font-family: ">: Inhibición; modelos cinéticos; hojas y cogollos; coctel de enzimas</span></p> <p class="MsoListParagraph" style="margin: 0cm; margin-bottom: .0001pt; mso-add-space: auto; text-align: justify; line-height: normal;"><strong style="mso-bidi-font-weight: normal;"><span style="font-size: 10.0pt; font-family: " lang="EN-US">Abstract: </span></strong><span class="hps"><span style="font-size: 10.0pt; font-family: " lang="EN-US">In this research, a delignified substrate from crops residues sugar cane residues (leaves and top cane) was hydrolyzed using an enzyme preparation with 27.53 FPU. This enzyme was obtained from trade. Hydrolysis was carried out to pH of 4.2 and a temperature of 50 <sup>o</sup>C. Models of inhibition models substrate, glucose and total inhibition product was analyzed. The results showed that models that best fit the data experimental was the models competitive glucose inhibition </span></span><span style="font-size: 10.0pt; font-family: " lang="EN-US">(K<sub>m</sub>= 20.37, V<sub>max</sub>=39 and k<sub>i</sub>= 0.442). In the event that E/S is above 0.5, can applied kinetic models of Michaelis – Menten.</span></p> <p class="MsoNormal" style="margin-bottom: .0001pt; text-align: justify; line-height: normal;"><strong style="mso-bidi-font-weight: normal;"><span style="font-size: 10.0pt; font-family: " lang="EN-US">Keywords</span></strong><span style="font-size: 10.0pt; font-family: " lang="EN-US">: Inhibition; <span class="apple-style-span">kinetic models</span></span><span class="apple-style-span"><span style="font-size: 10.0pt; mso-bidi-font-size: 11.0pt; font-family: ">; </span></span><span class="apple-style-span"><span style="font-size: 10.0pt; font-family: " lang="EN-US">leaves and tops cane</span></span><span class="apple-style-span"><span style="font-size: 10.0pt; mso-bidi-font-size: 11.0pt; font-family: ">; </span></span><span class="apple-style-span"><span style="font-size: 10.0pt; font-family: " lang="EN-US">enzyme cocktail.</span></span></p> <!--[if gte mso 9]><xml> <w:LatentStyles 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