Synthesis of a hybrid polymer-inorganic biomimetic support incorporating in situ pectinase from Aspergillus niger ATCC 9642

Bustamante-Vargas, Cindy Elena; Mignoni, Marcelo Luís; Oliveira, Débora de; Venquiaruto, Luciana Dornelles; Valduga, Eunice; Toniazzo, Geciane; Dallago, Rogério Marcos

doi:10.1007/s00449-015-1399-2

Cited by 4 publications

(2 citation statements)

References 36 publications

(43 reference statements)

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“…This may be due to the fact that the structure of SDP tends to be stable at the presence of the imprinting substrate, which facilitates the cross-linking reaction and results in an increased Schiff base. The disappearance and significant decrease of these characteristic peaks of MPs in immobilized SDP after immobilization indicates that the imprinting substrate has been removed and the enzyme activity center is released (Silva et al 2012;Bustamante-Vargas et al 2015;Chauhan et al 2015;Chakraborty et al 2016;Sojitra et al 2017). The circular dichroism (CD) spectra of DP and SDP are shown in Fig.…”

Section: Structural Characterization Of Sdpmentioning

confidence: 99%

“…In addition, imprinting with universal substrate (modified pectin) improved the substrate selection spectrum of the enzyme. Compared with DP, the substrate selection range of SDP was broader, which led to higher catalytic performance of SDP than DP to degrade pectin in whitewater and reduced its demand for cation (Li et al 2007;Bustamante-Vargas et al 2015).…”

Section: Effect Of Sdp On Pectin Substances In Whitewatermentioning

confidence: 99%

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Modified pectin as imprinting substrate to immobilize pectinase via both adsorption and crosslinking

Xiao

Sun

et al. 2019

BioRes

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A broad-spectrum substrate-imprinted adsorption and crosslinking double immobilized pectinase (SDP) was prepared using a universal modified pectin obtained through enzymatic hydrolysis as the imprinting substrate. Its structure was characterized by infrared spectroscopy, circular dichroism, and scanning electron microscopy. The results showed that 1) cross-linking increased the Schiff base in SDP, 2) immobilization barely changed the secondary structure such as α-helix and β-sheet of SDP, and 3) adhesives were evenly distributed on the surface after immobilization. Studies on the enzymatic properties of SDP showed that the substrate imprinting significantly improved heat resistance and neutralization resistance of SDP. For example, the relative activity of SDP at 35 to 75 °C and at pH 4.4 to 6.5 was 5% and 15% more than that of the adsorption and crosslinking double immobilized pectinase (DP), respectively. In addition, after 8 cycles of use, the relative enzyme activity of SDP still reached 39.5%. Moreover, use of SDP decreased the cation demand in whitewater by 10% compared with DP. Overall, the use of a broad-spectrum substrate for imprinting to obtain SDP provides a new idea and method for using pectinase in in complex systems such as juice clarification and wastewater treatment.

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Section: Structural Characterization Of Sdpmentioning

confidence: 99%

Section: Effect Of Sdp On Pectin Substances In Whitewatermentioning

confidence: 99%

Modified pectin as imprinting substrate to immobilize pectinase via both adsorption and crosslinking

Xiao

Sun

et al. 2019

BioRes

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Biomimetic Mineralization of the Alginate/Gelatin/Calcium Oxalate Matrix for Immobilization of Pectinase: Influence of Matrix on the Pectinolytic Activity

Bustamante-Vargas

Oliveira

Valduga

et al. 2016

Appl Biochem Biotechnol

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Pectinases catalyze the degradation of pectic substances and are used in several processes, mainly in food and textile industries. In this study, a biomimetic matrix of alginate/gelatin/calcium oxalate (AGOCa) was synthesized for the in situ immobilization via encapsulation of crude pectinase from Aspergillus niger ATCC 9642, obtaining an immobilization efficiency of about 61.7 %. To determine the performance of AGOCa matrix, this was compared to control matrices of alginate/calcium oxalate (AOxal) and alginate/water (ACa). By the evaluation of pH and temperature effects on the enzyme activity, it was observed an increase on pectinolytic activity for both three tested matrices with an increase on pH and temperature. The kinetic parameters for pectinase immobilized in the three matrices were determined using citric pectin as substrate. Values of K m of 0.003, 0.0013, and 0.0022 g mL(-1) and V max of 3.85, 4.32, and 3.17 μmol min(-1) g(-1) for AGOCa, AOxal, and ACa matrices were obtained, respectively. After 33 days of storage, the pectinase immobilized in the three different matrices kept its initial activity, but that immobilized in AGOCa presented high stability to the storage with a relative activity of about 160 %. The enzyme immobilized in AGOCa, AOxal, and ACa could be used in 10, 8, and 7 cycles, respectively, keeping 40 % of its initial activity.

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Liquefied petroleum gas as solvent medium for the treatment of immobilized pectinases

Gaio

Oro

Graboski

et al. 2017

Biocatalysis and Agricultural Biotechnology

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Synthesis of a hybrid polymer-inorganic biomimetic support incorporating in situ pectinase from Aspergillus niger ATCC 9642

Cited by 4 publications

References 36 publications

Modified pectin as imprinting substrate to immobilize pectinase via both adsorption and crosslinking

Modified pectin as imprinting substrate to immobilize pectinase via both adsorption and crosslinking

Biomimetic Mineralization of the Alginate/Gelatin/Calcium Oxalate Matrix for Immobilization of Pectinase: Influence of Matrix on the Pectinolytic Activity

Liquefied petroleum gas as solvent medium for the treatment of immobilized pectinases

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