TY - JOUR
T1 - Optimization of substrate composition for pectinase production from Satkara (Citrus macroptera) peel using Aspergillus niger-ATCC 1640 in solid-state fermentation
AU - Ahmed, Tanvir
AU - Rana, Md Rahmatuzzaman
AU - Zzaman, Wahidu
AU - Ara, Rowshon
AU - Aziz, Mohammad Gulzarul
N1 - Publisher Copyright:
© 2021 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/bync-nd/4.0/)
PY - 2021/10
Y1 - 2021/10
N2 - Pectinase is an enzyme having a broad industrial and commercial application. However, higher production costs may be the major constraint for the wide-scale application of pectinase. Therefore, researchers are trying to reduce the pectinase production cost for subsequent application in the industrial processes by using a unique substrate and optimizing the fermentation medium components and process conditions. The main purpose of the current study was to optimize medium composition for pectinase production using Aspergillus niger-ATCC 1640 in the solid-state fermentation.The Response Surface Methodology (RSM) was performed to evaluate the effects of variables, specifically the concentrations of Satkara peel, urea, (NH4)2PO4, NH4NO3, KH2PO4, ZnSO4, and MgSO4.7H2O on pectinase production in the solid substrate. Firstly, a two-factorial design, Plackett-Burman design (PBD) was applied to screen the variables that significantly influenced the pectinase production. After finding the critical variables, 15 experimental runs were carried out using a Box-Behnken design (BBD) to derive a statistical model for optimizing the concentrations of the selected variables. The PBD model revealed that Satkara peel, urea, and (NH4)2SO4significantly affected the pectinase production. RSM results indicated that the predicted response for pectinase production was in good agreement with experimental data (R2 = 0.9836). Under the optimized condition of Satkara peel (8.4 g/L), urea (0.5 g/L), and (NH4)2SO4 (2.7 g/L), the pectinase activity was predicted to be 0.6178 μmol/mL. In the present study, the experimental pectinase production achieved 0.6045 μmol/mL.
AB - Pectinase is an enzyme having a broad industrial and commercial application. However, higher production costs may be the major constraint for the wide-scale application of pectinase. Therefore, researchers are trying to reduce the pectinase production cost for subsequent application in the industrial processes by using a unique substrate and optimizing the fermentation medium components and process conditions. The main purpose of the current study was to optimize medium composition for pectinase production using Aspergillus niger-ATCC 1640 in the solid-state fermentation.The Response Surface Methodology (RSM) was performed to evaluate the effects of variables, specifically the concentrations of Satkara peel, urea, (NH4)2PO4, NH4NO3, KH2PO4, ZnSO4, and MgSO4.7H2O on pectinase production in the solid substrate. Firstly, a two-factorial design, Plackett-Burman design (PBD) was applied to screen the variables that significantly influenced the pectinase production. After finding the critical variables, 15 experimental runs were carried out using a Box-Behnken design (BBD) to derive a statistical model for optimizing the concentrations of the selected variables. The PBD model revealed that Satkara peel, urea, and (NH4)2SO4significantly affected the pectinase production. RSM results indicated that the predicted response for pectinase production was in good agreement with experimental data (R2 = 0.9836). Under the optimized condition of Satkara peel (8.4 g/L), urea (0.5 g/L), and (NH4)2SO4 (2.7 g/L), the pectinase activity was predicted to be 0.6178 μmol/mL. In the present study, the experimental pectinase production achieved 0.6045 μmol/mL.
KW - Box-Behnken design
KW - Enzymatic hydrolysis
KW - Pectinase
KW - Response surface methodology
KW - Utilization of Satkara peel
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U2 - 10.1016/j.heliyon.2021.e08133
DO - 10.1016/j.heliyon.2021.e08133
M3 - Article
C2 - 34693058
AN - SCOPUS:85120920685
SN - 2405-8440
VL - 7
JO - Heliyon
JF - Heliyon
IS - 10
M1 - e08133
ER -