Joni Agustian, Lilis Hermida, Heri Rustamaji, Muhammad Haviz

Glukoamilase amobil pada silika mesostructured cellular foam (mcf) magnetik untuk hidrolisis pati kentang

Introduction

Glukoamilase amobil pada silika mesostructured cellular foam (mcf) magnetik untuk hidrolisis pati kentang. Inovasi glukoamilase amobil pada silika MCF magnetik untuk hidrolisis pati kentang. Efisiensi imobilisasi mencapai 89,46% dengan DE optimum 26,93%, menjanjikan untuk aplikasi industri pangan.

Abstract

Inovasi dan studi silika mesopori magnetik untuk penyangga imobilisasi enzim glukoamilase untuk hidrolisis pati kentang belum dilakukan karena penyangga magnetik hanya dikaitkan dengan bahan partikel nano baik murni maupun komposit. Proses imobilisasi enzim glukoamilase pada penyangga dengan kondisi operasi proses divariasikan untuk diketahui pengaruhnya terhadap proses dimana hasil akhir adalah tingkat imobilisasi enzim yang cukup besar yang disimpulkan dari hasil analisis kandungan protein (metode Bradford), FTIR dan SEM-EDX. Bahan partikel nano magnetik berhasil diinkorporasi pada permukaan silika MCF (9.2T-3D) dengan tingkat imobilisasi optimum enzim glukoamilase bebas adalah sekitar 89,46% yang didapatkan pada kondisi operasi optimum pH larutan buffer 5,0, suhu operasi 35°C, kecepatan pengadukan 120 rpm,dan konsentrasi enzim suplai sebesar 5,5%. Walaupun unit aktivitas enzim amylase amobil adalah lebih rendah daripada enzim amylase bebas, enzim amobil tetap dapat digunakan untuk menghidrolisis susbtrat larut dalam air. Poses hidrolisis pati kentang dengan enzim tersebut menghasilkan nilai DE optimum 26,93% pada suhu 70°C, kecepatan pengadukan 170 rpm, pH buffer asetat 0,1 M 4,6, dan konsentrasi enzim 1500 U/mg.

Review

This manuscript presents an investigation into the immobilization of glucoamylase onto a novel magnetic mesostructured cellular foam (MCF) silica for the hydrolysis of potato starch. The authors highlight a significant gap in current research, noting that magnetic supports for enzyme immobilization are predominantly associated with nanoparticle-based materials rather than mesoporous silica. This work aims to bridge this gap by exploring the potential of magnetic MCF silica as an effective carrier, systematically varying immobilization conditions to optimize the process and characterize the resulting biocatalyst. The study successfully demonstrates the incorporation of magnetic nanoparticles onto the MCF silica surface, creating a robust and potentially reusable support. A high immobilization efficiency of approximately 89.46% for glucoamylase was achieved under optimized conditions, including a buffer pH of 5.0, a temperature of 35°C, and an agitation speed of 120 rpm. This substantial immobilization yield, supported by comprehensive characterization through protein content analysis (Bradford), FTIR, and SEM-EDX, underscores the effectiveness of the chosen support material and immobilization strategy. Although the specific activity of the immobilized enzyme was reported to be lower than that of the free enzyme, the immobilized glucoamylase remained highly effective in hydrolyzing water-soluble substrates, yielding an optimum Dextrose Equivalent (DE) of 26.93% for potato starch hydrolysis under specific operational parameters (70°C, 170 rpm, pH 4.6). While the work successfully demonstrates the feasibility of using magnetic MCF silica for glucoamylase immobilization, the reported lower unit activity of the immobilized enzyme compared to its free counterpart suggests an area for future improvement. Further investigations could explore alternative immobilization strategies or surface modifications of the MCF silica to enhance enzyme activity retention. Additionally, a more detailed discussion on the stability, reusability, and potential for industrial application of the immobilized enzyme, particularly regarding the achieved DE value, would strengthen the manuscript. Nevertheless, this study represents a valuable contribution to the field of biocatalyst development, presenting a promising novel magnetic mesoporous support for glucoamylase and laying foundational work for the efficient hydrolysis of potato starch.

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