Immobilization of fenugreek β-amylase onto functionalized graphene quantum dots (GQDs) using Box-Behnken design: Its biochemical, thermodynamic and kinetic studies

Agrawal, Dinesh Chand; Yadav, Anjali; Kesarwani, Rashmi; Srivastava, O. N.; Kayastha, Arvind M.

doi:10.1016/j.ijbiomac.2019.12.033

Cited by 39 publications

(20 citation statements)

References 72 publications

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“…The 11 BioMed Research International [46]. BBD is a diverse approach that involves answer optimization based on various variable methods, including mathematical and statistical methods [30]. BBD was utilized to optimize the culture conditions for α-amylase generation, and a value of 145.32 U/ml of amylase was obtained [47].…”

Section: Discussionmentioning

confidence: 99%

“…Yahya et al reported that conditions in fungal strain A. tubingensis SY1 extracellular amylase production were factually optimized using the Plackett-Burman equation, with the most significant variables of amylase production being peptone, agitation, and MgSO 4 ·7H 2 O followed by inoculum size [ 46 ]. BBD is a diverse approach that involves answer optimization based on various variable methods, including mathematical and statistical methods [ 30 ]. BBD was utilized to optimize the culture conditions for α -amylase generation, and a value of 145.32 U/ml of amylase was obtained [ 47 ].…”

Section: Discussionmentioning

confidence: 99%

“…After assessing the relative importance of the discrete variables, the four most important variables were chosen to determine the optimum levels for α -amylase enzyme development. The Box-Behnken design (BBD) was used because it is a surface response methodology ( Table 3 ) [ 29 , 30 ]. This optimization method includes three key steps: coefficient estimation of the mathematical model, response prediction, and model adequacy verification.…”

Section: Methodsmentioning

confidence: 99%

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Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes

Al-Agamy

Alhuzani

Kelany

et al. 2021

BioMed Research International

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Amylase producing actinobacteria were isolated and characterized from terrestrial environment. There are a limited number of reports investigating the marine environment; hence, in the present study, four marine enzymes were tested for their amylase production ability. On starch agar plates, the Streptomyces rochei strain showed a higher hydrolytic zone (24 mm) than the other isolates. Growth under optimized culture conditions using Plackett-Burman’s experimental design led to a 1.7, 9.8, 7.7, and 3.12-fold increase for the isolates S. griseorubens, S. rochei, S. parvus, and Streptomyces sp., respectively, in the specific activity measurement. When applying the Box-Behnken design on S. rochei using the most significant parameters (starch, K2HPO4, pH, and temperature), there was a 12.22-fold increase in the specific activity measurement 7.37 U/mg. The α-amylase was partially purified, and its molecular weight was determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. α-Amylase was particularly active at pH 6 and 65°C. The purified enzyme was most active at 65°C and pH 6, thermal stability of 70°C for 40 min, and salt concentration of 1 M with Km and Vmax of 6.58 mg/ml and 21.93 μmol/ml/min, respectively. The α-amylase was improved by adding Cu+2, Zn+2, and Fe+2 (152.21%, 207.24%, and 111.89%). Increased production of α-amylase enzyme by S. rochei KR108310 leads to production of significant industrial products.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes

Al-Agamy

Alhuzani

Kelany

et al. 2021

BioMed Research International

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“…The analysis of variance (ANOVA) with a confidence level of 95% was also generated by Design Expert (Version 11) to test the significance of factors and the accuracy of models. For the Box–Behnken design, a quadratic model is selected to show the relationship between the factors and the response as the following format:

y = c_{0} + \sum_{i = 1}^{m} c_{i} x_{i} + \sum_{i = 1}^{m} c_{i i} x_{i}^{2} + \sum_{i = 1}^{m} \sum_{j = 1}^{m} c_{i j} x_{i} x_{j} + c_{1}

where

y

c_{0}

c_{i}

c_{i i}

c_{i j}

x_{i}

x_{j}

, and

c_{1}

represent predicted responses, offset constant, coefficient of linear terms, coefficient of quadratic terms, coefficient of interaction terms,

i

th factor,

j

th factor, and the random error between predicted values and measured values, respectively [15]. RSM was applied for the numerical optimization of factors.…”

Section: Methodsmentioning

confidence: 99%

Parametric optimization and kinetic study of l‐lactic acid production by homologous batch fermentation of Lactobacillus pentosus cells

Wang

Huang

Jiang

et al. 2020

Biotech and App Biochem

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Parametric optimization always plays important roles in bioengineering systems to obtain a high product yield under the proper conditions. The parametric conditions of lactic acid production by homologous batch fermentation of Lactobacillus pentosus cells was optimized by the Box–Behnken design. The highest l‐lactic acid yield was obtained as 0.836 ± 0.003 g/g glucose with the productivity of 0.906 ± 0.003 g/(L × H) under the optimum conditions of 34.7 °C, pH 6.2, 148 rpm agitation speed, and 9.3 g/L nitrogen source concentration determined by quadratic response surface with high accuracy. The adequate kinetic models of cell growth rate, lactic production rate, and glucose consumption rate were also established to describe the fermentation behavior of L. pentosus cells with the correlation coefficients of 09985, 0.9990, and 0.9989, respectively.

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“…The positive ΔS observed for the immobilized enzyme (Table 3) is directly indicative of protein unfolding (greater disorder) during inactivation. [72][73] By contrast, the corresponding negative ΔS values for the free enzyme can be related to the formation of protein aggregates during inactivation as a result of denaturation. The aggregates are less disordered compared to the soluble proteins moving freely in the solution, hence the negative ΔS values.…”

Section: Ea (Kj Mol -1 )mentioning

confidence: 97%

Improving β-Galactosidase-Catalyzed Transglycosylation Yields by Cross-Linked Layer-by-Layer Enzyme Immobilization

Alavijeh

Meyer

Gras

et al. 2020

ACS Sustainable Chem. Eng.

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The biotransformation of lactose into gut-bioactive glycans catalyzed by βgalactosidase can give economic value to lactose-rich side streams generated in the food or dairy industry. Herein, we study the immobilization of the commercially used β-galactosidase from Bacillus circulans onto silica particles using an enzyme immobilization technology involving a cross-linked layer-by-layer encapsulation method. The immobilized β-galactosidase was used for the synthesis of Nacetyllactosamine (LacNAc) as an important precursor for numerous bioactive compounds and a prebiotic in itself. Techniques including molecular analysis, enzyme activity determination, secondary structure analysis, thermodynamic characterization as well as the determination of thermal and operational stability were conducted to characterize the immobilized enzyme. Changes in the activity of the enzyme after immobilization were attributed to possible changes in electrostatic, covalent and protein-protein interactions. Immobilization significantly improved enzymatic LacNAc yield compared to the free enzyme. In turn, this improved the economics and the sustainability of the process. The immobilized enzyme encapsulated in multilayer films was significantly more stable in the presence of divalent cations and its thermostability also substantially increased, with the thermal denaturation activation energy increasing from 53 kJ mol -1 to 294 kJ mol -1 . The immobilized enzyme was successfully reused in eight consecutive reaction cycles with no significant reduction in the LacNAc yield. The improved transgalactosylation yield and productivity, higher stability and reusability obtained with this immobilization method provide new opportunities for industrial applications.

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Immobilization of fenugreek β-amylase onto functionalized graphene quantum dots (GQDs) using Box-Behnken design: Its biochemical, thermodynamic and kinetic studies

Cited by 39 publications

References 72 publications

Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes

Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes

Parametric optimization and kinetic study of l‐lactic acid production by homologous batch fermentation of Lactobacillus pentosus cells

Improving β-Galactosidase-Catalyzed Transglycosylation Yields by Cross-Linked Layer-by-Layer Enzyme Immobilization

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