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Agustian, Joni
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Agriculture, Biological Sciences & Forestry Automotive Engineering Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Civil Engineering, Building, Construction & Architecture Computer Science & IT Education Electrical & Electronics Engineering Engineering Environmental Science Industrial & Manufacturing Engineering Medicine & Pharmacology Social Sciences Other

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Journal : Bulletin of Chemical Reaction Engineering

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The Optimised Statistical Model for Enzymatic Hydrolysis of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica Joni Agustian; Lilis Hermida
Bulletin of Chemical Reaction Engineering & Catalysis 2019: BCREC Volume 14 Issue 2 Year 2019 (August 2019)
Publisher : Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.9767/bcrec.14.2.3078.380-390

Abstract

Enzymatic hydrolysis of starches using free glucoamylase to reducing sugars have difficulties in recovering and recycling of the enzyme, hence immobilisation on inert supports were widely studied. However, effectiveness of the immobilised glucoamylase were merely observed only on soluble starches. It was considered a valuable thing to know performance of glucoamylase on Mesostructured Cellular Foam (MCF) silica in hydrolysing of tapioca. An optimised study on enzymatic hydrolysis of tapioca using glucoamylase on MCF silica (9.2T-3D) and its kinetics were described including justification of the predicted model as it was required to develop in large scale operations. Central Composite Design was used to model the process by studying effects of three factors on DE values after enzyme immobilisation.  Immobilisation of glucoamylase on this support gave up to 82% efficiency with the specific activity of 1,856.78 U.g-1. Its used to hydrolysis of tapioca resulted DE values of 1.740-76.303% (w/w) where the highest DE was obtained at pH of 4.1, temperature of 70 ℃ and agitation speed of 140 rpm. The optimisation produced a polynomial quadratic model having insignificant lack-of-fit and low standard deviation, so that it was applicable and reliable in simulating the DE with only 0.80% of data were not described. Temperature affected the process highly, but the buffer pH, agitation speed and factorial interactions were considered not important. KM value for immobilised enzyme was better than the free glucoamylase, however, its reaction rate was slower than the free glucoamylase catalysis. Copyright © 2019 BCREC Group. All rights reserved 
Salt-Assisted Mesostructured Cellular Foam (MCF) Silica Synthesis from Bagasse Bottom Ash for Enzymatic Starch Hydrolysis Agustian, Joni; Hermida, Lilis
Bulletin of Chemical Reaction Engineering & Catalysis 2025: BCREC Volume 20 Issue 3 Year 2025 (October 2025)
Publisher : Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.9767/bcrec.20379

Abstract

Synthesis of MCF silica is presently conducted solely using TEOS and TMB, with the purpose of immobilizing amylolytic enzymes.  Utilizing BBA and KCl to create the salt-assisted MCF silica present a viable option for converting a natural waste into an effective enzyme carrier, given its substantial silica content.  The objectives were to produce the MCF silica, to employee the MCF silica as the glucoamylase carrier, and to know characteristics of the immobilized enzyme by conducting hydrolysis of starches.  The carrier had surface area of 45.5 m2 g-1, pore volume of 0.12 cm3 g-1, pore size of 9.3 nm, and mesoporous silica type IV.  Reduction in the carrier pore diameter and the medium to strong FTIR vibrations indicated free glucoamylase immobilization on carrier.  The immobilization reached 88.5% efficiency, influenced by factors such as initial enzyme concentration, PO₄ buffer pH, and temperature, with agitation speed having a minor impact.  This optimum value was obtained at the initial enzyme concentration of 9.0 mg mL-1, agitation speed of 120 rpm, buffer pH of 5.5, and temperature of 30°C.  Hydrolysis of starches (tapioca, wheat, potato, corn) resulted in Dextrose Equivalent (DE) values ranging from 5.1% to 63.9%, with the immobilized glucoamylase showing better performance in potato starch hydrolysis (DE of 63.9%) and corn starch (DE of 45.6%).  The use of BBA in synthesis of the salt-assisted MCF silica proved to be a viable and sustainable alternative for enzyme immobilization, with potential applications in industrial starch hydrolysis.
Co-Authors Ade Febriana Syahfitri Anggraini, Devi Sagitha Dwi Herianto Elida Purba Heri Rustamaji Hermida, Lilis Kurniasari, Bela M. Haviz Pia Sabrina Murtadho Yunita Kesuma Zahratul Azizah