Immobilization of α - amylase from locale bacteria isolate Bacillus subtilis ITBCCB148 with diethylaminoethyl cellulose (DEAE-Cellulose)

Yandri,; Suhartati, Tati; Hadi, Sutopo

doi:10.13005/msri/070114

Cited by 8 publications

(7 citation statements)

References 15 publications

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“…Some previous researches performed with immobilization and chemical modification have shown that the enzymes obtained have significantly increased their stability against pH and temperature compared to the native enzyme (Yandri, et al, 2008(Yandri, et al, , 2010a(Yandri, et al, , 2010bGermain dan Crichton, 1988;Cordt, et al, 1992;Steadman, et al, 1991;Skerker dan Clark, 1987;Rani, et al, 2007;Reshmi, et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of a-Amylase from Locale Bacteria Isolate Bacillus subtilis ITBCCB148 with Carboxymethyl Cellulose (CM-Cellulose)

Yandri¹,

Susanti²,

Suhartati³

et al. 2012

MAS

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This paper describes the stability increase of α-amylase obtained from Bacillus subtilis ITBCCB 148 by immobilization process using carboxymethyl cellulose (CM-Cellulose) as the immobile matrix. To achieve this aim the enzyme was purified by the following steps: fractionation with ammonium sulphate, dialysis, ion exchange column chromatography with CM-cellulose and molecule filtration column chromatography with Sephadex G-100. The purified enzyme was then immobilized with CM-Cellulose. The result showed that the immobilization with CM-cellulose on α-amylase obtained from B. subtilis has successfully increased the thermal stability of the native enzyme. The thermal stabilities of the modified enzyme were increased 3.67 times compared to the native enzyme. The decrease of ki value, the increase of half-life and ΔGi values showed that the modified enzymes were more stable than the native enzyme.

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Section: Introductionmentioning

confidence: 99%

“…The binding in the adsorption method is normally occurred by ionic and covalent bond. The uses of support matrix containing either anionic or cationic exchange residues as immobile matrix has some advantages as the bond formed is relatively stable (Yandri, et al, 2010b).…”

Section: Introductionmentioning

confidence: 99%

Immobilization of a-Amylase from Locale Bacteria Isolate Bacillus subtilis ITBCCB148 with Carboxymethyl Cellulose (CM-Cellulose)

Yandri¹,

Susanti²,

Suhartati³

et al. 2012

MAS

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“…Immobilization process on -amylase from B.subtilis ITBCCB148 has successfully increased the enzyme stability at high temperature using diethylaminoethyl cellulose (DEAE-Cellulose) 8 ; carboxymethyl cellulose (CM-Cellulose) 9 ; and bentonite 10, 11 , calcium alginate 12 although the increase was only 1.5; 3.67 and 2.12, however, the immobilized enzymes could be used between 5-6 times. Immobilization on -amylase has also been performed using amberlite 13 and gelatin 14 where they have successfully increased the stability of this enzyme.…”

Section: Introdcutionmentioning

confidence: 99%

Increasing Stability of a-amylase Obtained from Bacillus subtilis ITBCCB148 by Immobilization with Chitosan

Yandri¹,

Suhartati²,

Satria³

et al. 2020

Mediterr.J.Chem.,

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In this research, the immobilization of α-amylase from Bacillus subtilis ITBCCB148 by crosslinking method on chitosan matrix has been performed. This research aims to know the effect of immobilization on the thermal stability of α-amylase. The results showed that the native α-amylase has an optimum temperature of 65oC, KM = 1.6 mg mL-1 substrate, and Vmax = 39.7 µmol mL-1 min-1. The immobilized α-amylase has optimum temperature of 75oC, KM = 3.5 mg mL-1 substrate, and Vmax = 7.05 µmol mL-1 min-1. The residual activity of the native and immobilized enzyme on thermal stability test at 65oC for 80 minutes was 58% and 86.15%, respectively. The immobilized enzyme can be reused up to six repeated cycles.The thermodynamic data of native enzyme was t½ = 113.6 min, ki = 6.1x10-3 min-1, and ΔGi = 107.3 kJ mol-1, while the immobilized enzyme was t½ = 433.1 min, ki= 1.6x10-3 min-1, and ΔGi 111.1 kJ mol-1. Based on the decrease of ki, and the increase of ΔGi and half-life(t½) values, the immobilization of α-amylase with chitosan can increase the thermal stability of this enzyme.

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“…Research phases performed were production, isolation, purification and characterization of the purified (native) enzyme similar to the procedures previously reported 9 .…”

Section: Research Phasesmentioning

confidence: 99%

Increasing Stability of Cellulase, Obtained from Bacillus subtilis ITBCCB148 with Chemical Modification Using p-Nitrophenolcarbonate-Polyethylenglycol (NPC-PEG)

Yandri¹,

Amalia²,

Suhartati³

et al. 2017

Orient. J. Chem

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This research aims to increase the stabilty of cellulase obtained from local bacteria isolate Bacillus subtilis ITBCCB148 by chemical modification using p-nitrophenolcarbonate polyethylenglycol (NPC-PEG). The characterization of the native and modified enzymes were performed by determination of optimum pH and temperature as well as thermal stability. The result showed that the native enzyme has optimum temperature and pH is 55 o C and 6, respectively. The thermal stability test of native enzyme for 60 min. at temperature of 55 o C gave values of thermal inactivation rate constant (k i ) 0.035/min., half-life (t 1/2 ) 19.80 min. and denaturation energy ΔG i )= 100.908 kJ/mol. The modified enzymes with modification degree of 63, 70 and 81% have the same values of optimum temperature and pH as native enzyme, but their stability data have increased very significantly. Their k i values were 0.014; 0.012 and 0.011, respectively. Their t 1/2 values were 49.5; 57.75 and 63 min., respectively; and their ΔG i values were 103.407; 103.828 and 104.065 kJ/ mole, respectively. Thus, the chemical modification using NPC-PEG has shown to increase the enzyme stability of modified enzyme 2.5 -3.2 times compared to the native enzyme, although no change of optimum temperature and pH was observed

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Immobilization of α - amylase from locale bacteria isolate Bacillus subtilis ITBCCB148 with diethylaminoethyl cellulose (DEAE-Cellulose)

Cited by 8 publications

References 15 publications

Immobilization of a-Amylase from Locale Bacteria Isolate Bacillus subtilis ITBCCB148 with Carboxymethyl Cellulose (CM-Cellulose)

Immobilization of a-Amylase from Locale Bacteria Isolate Bacillus subtilis ITBCCB148 with Carboxymethyl Cellulose (CM-Cellulose)

Increasing Stability of a-amylase Obtained from Bacillus subtilis ITBCCB148 by Immobilization with Chitosan

Increasing Stability of Cellulase, Obtained from Bacillus subtilis ITBCCB148 with Chemical Modification Using p-Nitrophenolcarbonate-Polyethylenglycol (NPC-PEG)

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