577
Views
2
CrossRef citations to date
0
Altmetric
Research Article

Comparison of some biochemical properties of artichoke polyphenol oxidase entrapped in alginate-carrageenan and alginate gels

&
Pages 268-273 | Received 01 Apr 2013, Accepted 14 May 2013, Published online: 25 Jun 2013

Figures & data

Figure 1. The effect of pH on catecholase (A) and cresolase (B) activities of entrapped polyphenol oxidase in alginate gel and alginate+κ-carrageenan polymer blends.

Figure 1. The effect of pH on catecholase (A) and cresolase (B) activities of entrapped polyphenol oxidase in alginate gel and alginate+κ-carrageenan polymer blends.

Figure 2. The effect of temperature on catecholase (A) and cresolase (B) activities entrapped polyphenol oxidase in alginate gel and alginate+κ-carrageenan polymer blends.

Figure 2. The effect of temperature on catecholase (A) and cresolase (B) activities entrapped polyphenol oxidase in alginate gel and alginate+κ-carrageenan polymer blends.

Figure 3. Kinetic parameters of entrapped polyphenol oxidase in alginate gel and alginate+κ-carrageenan polymer blends for catecholase (A) and cresolase (B) activities.

Figure 3. Kinetic parameters of entrapped polyphenol oxidase in alginate gel and alginate+κ-carrageenan polymer blends for catecholase (A) and cresolase (B) activities.

Table I. Km and Vmax values of entrapped artichoke polyphenol oxidase into alginate and alginate+κ-carrageenan gel beads for catecholase and cresolase activities.

Figure 4. The thermal stabilities of entrapped PPOs in alginate+κ-carrageenan beads (A) and alginate beads (B) for catecholase activities. The free enzyme and beads were incubated for various time intervals (15–60 min) at the specified temperature (50–60°C) and rapidly cooled. The activity was measured at 25°C, was taken as 100% and activities measured (50–60°C) were compared with the activity measured at 25°C. Empty symbols show immobilized enzyme (solid line), filled symbols free enzyme (dotted line). Each value is a mean of duplicate experiments.

Figure 4. The thermal stabilities of entrapped PPOs in alginate+κ-carrageenan beads (A) and alginate beads (B) for catecholase activities. The free enzyme and beads were incubated for various time intervals (15–60 min) at the specified temperature (50–60°C) and rapidly cooled. The activity was measured at 25°C, was taken as 100% and activities measured (50–60°C) were compared with the activity measured at 25°C. Empty symbols show immobilized enzyme (solid line), filled symbols free enzyme (dotted line). Each value is a mean of duplicate experiments.

Figure 5. The thermal stabilities of entrapped PPOs in alginate+κ-carrageenan (A) and alginate gels (B) for cresolase activities. Empty symbols show immobilized enzyme (solid line), filled symbols free enzyme (dotted line). The free enzyme and beads were incubated for various time intervals (15–60 min) at the specified temperature (60–70°C) and rapidly cooled. The activity was measured at 25°C, was taken as 100% and activities measured (60–70°C) were compared with the activity measured at 25°C. Each value is a mean of duplicate experiments.

Figure 5. The thermal stabilities of entrapped PPOs in alginate+κ-carrageenan (A) and alginate gels (B) for cresolase activities. Empty symbols show immobilized enzyme (solid line), filled symbols free enzyme (dotted line). The free enzyme and beads were incubated for various time intervals (15–60 min) at the specified temperature (60–70°C) and rapidly cooled. The activity was measured at 25°C, was taken as 100% and activities measured (60–70°C) were compared with the activity measured at 25°C. Each value is a mean of duplicate experiments.

Figure 6. The storage stabilities of entrapped polyphenol oxidase in alginate gel and alginate+κ-carrageenan polymer blends for catecholase (A) and cresolase (B) activities.

Figure 6. The storage stabilities of entrapped polyphenol oxidase in alginate gel and alginate+κ-carrageenan polymer blends for catecholase (A) and cresolase (B) activities.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.