Agustian, Joni and Hermida, Lilis (2019) The Optimised Statistical Model for Enzymatic Hydrolysis of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica. Bulletin of Chemical Reaction Engineering & Catalysis, 14 (2). pp. 380-390. ISSN 1978-2993

Preview	Text 4 JAG Published Article.pdf Download (809kB) | Preview
	Text 3078 Download (68kB)

Abstract

Enzymatic hydrolysis of starches using free glucoamylase to reducing sugars have difficulties in recov-ering and recycling of the enzyme, hence immobilisation on inert supports were widely studied. Howev-er, 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 pre-dicted 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 immobilisa-tion. Immobilisation of glucoamylase on this support gave up to 82% efficiency with the specific activi-ty 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 op-timisation produced a polynomial quadratic model having insignificant lack-of-fit and low standard de-viation, 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 in-teractions 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.

Item Type:	Article
Subjects:	T Technology > TP Chemical technology
Divisions:	Fakultas Teknik (FT) > Prodi Teknik Kimia
Depositing User:	JONI AGUST
Date Deposited:	19 Mar 2020 00:48
Last Modified:	19 Mar 2020 00:48
URI:	http://repository.lppm.unila.ac.id/id/eprint/18783

Actions (login required)

View Item