“…This result was higher than the one obtained by ESCOBAR et al (2014), who immobilized K. lactis β-galactosidase in calcium alginate spheres and achieved a maximum lactose conversion of 40% during the same reaction time. The highest conversion obtained in this research may be attributed to the use of gelatin, which decreased swelling of the alginate spheres, minimizing the leaching of the enzyme from the support to the external medium (SHEN et al, 2011).…”
One of the greatest challenges for dairy industries is the correct destination of all the whey generated during cheese making, considering its high impact, the large volume created
“…This result was higher than the one obtained by ESCOBAR et al (2014), who immobilized K. lactis β-galactosidase in calcium alginate spheres and achieved a maximum lactose conversion of 40% during the same reaction time. The highest conversion obtained in this research may be attributed to the use of gelatin, which decreased swelling of the alginate spheres, minimizing the leaching of the enzyme from the support to the external medium (SHEN et al, 2011).…”
One of the greatest challenges for dairy industries is the correct destination of all the whey generated during cheese making, considering its high impact, the large volume created
“…The immobilization methodology used in this work was adapted from Shen et al [16]. Initially, a 2 % (p/v) sodium alginate solution dissolved in sodium oxalate buffer (100 mM, pH 5.5) was prepared.…”
Section: Immobilization Of the Pectinolytic Enzymatic Extractmentioning
confidence: 99%
“…Shen et al [16] used potassium phosphate buffer (100 mM, pH 7.5) to obtain a polymer-inorganic support for encapsulation of b-galactosidase. Preliminary tests performed here (data not shown) demonstrated that potassium phosphate buffer led to the total loss of activity for the pectinolytic extract.…”
Section: Screening Of Buffer For Immobilization Of the Pectinolytic Ementioning
The hybrid alginate/gelatin/calcium oxalate (AGOCa) support was successfully synthesized through the biomimetic mineralization method for immobilization in situ of a pectinolytic extract from Aspergillus niger ATCC 9642 via entrapment technique. The efficiency of immobilization reached 72.7%. Sodium oxalate buffer (100 mM, pH 5.5) was selected as adjuvant of the immobilization process by allowing the formation of a calcified shell around the calcium alginate capsule, significantly increasing the stability to storage, thermal and recycling of the enzymatic immobilized pectinolytic extract. The pH and temperature for maximum activity were from 5.0 to 6.0 and 60 to 80 °C, respectively. The new hybrid support can be a potential alternative to obtain immobilized pectinases with properties for advantageous industrial applications.
“…To overcome this limitation, researchers have adopted many methods, one of which is to modify the support surface with biofriendly molecules to obtain the biocompatible surface to reduce the enzyme denaturation during the immobilization [32][33][34]. There are many methods to form such biocompatible ("bio-friendly") support surfaces, including coating, adsorption, and self-assembly [35,36].…”
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