Coconut fibers

Effects of different levels of coconut fiber on blood glucose, serum insulin, and minerals in rats. Indian J Physiol Pharmacol 2000 44(1) 97-100. 

Coconut Fiber Dynamite It was obtd in 1905 by Gonsalves by soaking coconut fibers in NG. It was claimed that this dynamite was not affected by low temps Ref Clift St Fedoroff 2 (1943), pCl 2... 

The plants in the container will then develop two separate root systems. The upper root system will use any hydroponic medium you wish other than lava rock, which is used on the bottom half. I recommend that you use rockwool, coconut fiber, composted bark, Oasis fiber, peat perlite, and vermiculite, or my standard suggested "soil" formula for the upper medium layer. You may use... 

Because the E F method is medium friendly, a variety of growing mediums may be used during all stages of growth - from clones, to pre-bloomers, to blooming plants, I prefer the standard medium of perlite/vermiculite/potting soil. However, inert media such as rockwool, perlite, or coconut fiber work just as well. The standard medium is more versatile because it is easy to obtain. 

The containers used for the semi-organic grow beds are standard hydroponic grow containers. The medium used is any basic hydroponic medium. You will not use the standard medium of perlite/vermiculite/potting soil that was used with the total organic grow process because the medium will leach into the water. Use only standard hydroponic materials such as lava rock, hydroponic rock, rockwool, perlite, coconut fiber, or coir fiber. Fill the container to the top (as opposed to only /a full as is done with the totally organic method) with any hydroponic medium you prefer. 

Medium of choice, such as rockwool cubes, lava rock, perlite/vermiculite mixture, loose rockwool, or coconut fiber... 

Immobilization of Candida Antarctica Lipase B by Adsorption to Green Coconut Fiber... 

Abstract An agroindustrial residue, green coconut fiber, was evaluated as support for immobilization of Candida antarctica type B (CALB) lipase by physical adsorption. The influence of several parameters, such as contact time, amount of enzyme offered to immobilization, and pH of lipase solution was analyzed to select a suitable immobilization protocol. Kinetic constants of soluble and immobilized lipases were assayed. Thermal and operational stability of the immobilized enzyme, obtained after 2 h of contact between coconut fiber and enzyme solution, containing 40 U/ml in 25 mM sodium phosphate buffer pH 7, were determined. CALB immobilization by adsorption on coconut fiber promoted an increase in thermal stability at 50 and 60 °C, as half-lives (t /2) of the immobilized enzyme were, respectively, 2- and 92-fold higher than the ones for soluble enzyme. Furthermore, operational stabilities of methyl butyrate hydrolysis and butyl butyrate synthesis were evaluated. After the third cycle of methyl butyrate hydrolysis, it retained less than 50% of the initial activity, while Novozyme 435 retained more than 70% after the tenth cycle. However, in the synthesis of butyl butyrate, CALB immobilized on coconut fiber showed a good operational stability when compared to Novozyme 435, retaining 80% of its initial activity after the sixth cycle of reaction. 

Keywords Candida antarctica lipase B Enzyme immobilization Coconut fiber ... 

Thus, in order to produce a low-cost immobilized lipase, the objective of this work is to evaluate the immobilization of CALB by adsorption on green coconut fiber. For this purpose, the influence of contact time, lipase concentration, and pH of lipase solution during the adsorption step on the biocatalyst activity and stability was investigated. 

Green coconut fiber was obtained from green coconut husk through a process developed by Embrapa Agroindustria Tropical [28]. It was cut and sieved to obtain particles between 32 and 35 mesh. It was then washed with distilled water and dried at 60 °C before being used as immobilization matrix. 

Immobilization of C. antarctica Lipase B on Coconut Fiber by Adsorption... 

Adsorption kinetic was investigated, and the influence of contact time between coconut fiber and lipase, at different enzyme concentrations from 0 U/ml (control without enzyme) to 90 U/ml, were evaluated. No hydrolytic activity was detected when the fiber without immobilized enzyme (control) was used as catalyst. Figure 1 pictures the influence of different initial concentrations of lipase in the supernatant ( 0 equal to 30, 60, or 90 U/ml) on the hydrol)ftic activity of immobilized CALB. The experimental data were subjected to statistical analysis (analysis of variance). At the probability level of p<0.05 (data not shown), it was observed that immobilized amount increases as time increased until 2 h (in... 

Fig. 1 Effect of contact time on the hydrolytic activity of lipase immobilized on coconut fiber by adsorption using initial enzyme concentrations of 30 U/ml (closed triangle), 60 U/ml (closed circle), or 90 U/ml (closed square)...

In subsequent experiments, to evaluate the influence of enzyme loading on the properties of the immobilized enzyme, contact time was set in 2 h, and enzyme concentration in the supernatant, during incubation, was changed from 30 to 500 U/ml (Fig. 2). It can be seen that hydrolytic activity of the immobilized enzyme enhances with increasing lipase concentration in the supernatant. However, the higher value of hydrolytic activity achieved by adsorption of CALB on coconut fiber (135.14 U/g) was still lower than the hydrolytic activity of Novozyme 435 (1,039 U/g, determined according to the methodology described in Assay of Hydrolytic Activity Methyl Butyrate Hydrolysis ), a commercial derivative. 

Nevertheless, when higher concentrations of lipase in the supernatant were used, Eo= 150 U/ml, recovered activity decreased, and immobilization yield was enhanced (Table 1). According to the literature [4, 6, 9, 10], protein adsorption is not restricted to a monolayer on the support, and adsorption of secondary layers has been reported. Therefore, when Eo= 150 U/ml, probably a second layer of lipase was adsorbed on the first layer, leading to an improvement on immobilization yield, as more enzyme molecules were adsorbed. However, although more molecules were immobilized on coconut fiber, not all of them... 

CALB immobilized by adsoiption on coconut fiber at pH 7 and room temperature... 

In order to evaluate the formation of enzyme multilayers [10], thermal stability studies of lipase immobilized in coconut fiber, obtained by using ])=40 U/ml or o=280 U/ml, were performed at 60 °C. The thermal deaetivation model (Eq. 2) was fitted to experimental data (Fig. 5), and the model parameters are listed in Table 2. 

Table 2 Kinetics parameters of thermal deactivation, at 50 and 60 °C, of soluble CALB, CALB immobilized by adsorption on coconut fiber and Novozyme 435. ...

CALB-7A CALB immobilized by adsorption on coconut fiber at pH 7, using b=40 U/ml CALB-7B CALB immobilized by adsorption on coconut fiber at pH 7, by using o=280 U/ml CALB-4A CALB immobilized by adsorption on coconut fiber at pH 4, by using E(,=40 U/ml CALB-5A CALB immobilized by adsorption on coconut fiber at pH 5, by using o=40 U/ml. 

Although the amount of C. antarctica lipase type B adsorbed to coconut fiber was nearly independent on the pH of adsorption (between pH 3 and 6), immobilization yield and recovered activity were dependent on the pH of adsorption because interactions between the molecule and its environment influence the structure of a protein molecule, and these interactions are pH-dependent [8],... 

Fig. 3 Effect of the pH of immobilization on the amount of adsorbed protein (closed circle) and on the hydrolytic activity (open square). Lipase was immobilized on coconut fiber by adsorption after 2 h of contact time at room temperature...

Based on the obtained results, immobilized enzyme prepared at pH 4 (CALB-4) and 5 (CALB-5) were selected for thermal stability studies at 60 °C. Table 2 shows the kinetic parameters of thermal deactivation at 60 °C estimated by fitting deactivation model, Eq. 2, to experimental data. It can be observed that the deactivation profiles of CALB-4 and CALB-5 were similar, as ki and 2 are almost the same. However, by comparing the half-lives of CALB-4 and CALB-5 to CALB-7A, it can be observed that the biocatalyst prepared at pH 7 is 3- and 3.8-fold more stable than the ones prepared at pH 4 and 5, respectively. Considering that CALB has an optimum pH between 7 and 8 [35], when the enzyme is adsorbed on coconut fiber at pH 7, a favorable molecule conformation is preserved, being, therefore, more thermal stable than CALB-4 and CALB-5. Therefore, lipase immobilized at pH 7 was selected for fiirther kinetic, operational, and thermal stability studies. 

Based on the results obtained so far, CALB-7A, CALB immobilized on coconut fiber after 2 h of contact between the support and an enzyme solution containing Eo=40 U/ml, in... 

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