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All Journal Indonesian Journal of Pharmaceutical Science and Technology Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology
NANDYAWATI, DEWI
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Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Computer Science & IT Environmental Science Immunology & microbiology Medicine & Pharmacology

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Immobilization of Penicillin-G Acylase from Bacillus thuringiensis BD1 for Enhanced Amoxicillin Production Using Na-Alginate Entrapment Dewi, Rizky Aulia Prasasti; Widyasti, Erma Widyasti; Dianursanti, Dianursanti; Sriherwanto, Catur; Kusumaningrum, Susi; Rahayu, Maya D.; Putra, Noorendra L.; Hasanah, Nuur F.; Sativa, Rizka G.; Setyahadi, Siswa; Nandyawati, Dewi
Indonesian Journal of Pharmaceutical Science and Technology Vol 12, No 3 (2025)
Publisher : Indonesian Journal of Pharmaceutical Science and Technology

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.24198/ijpst.v12i3.55501

Abstract

Efficient enzymatic production, particularly using Penicillin-G Acylase (PGA), is crucial for synthesizing amoxicillin, a penicillin-type antibiotic. This study optimized PGA immobilization from Bacillus thuringiensis BD1 using Na-alginate to enhance stability and cost-effectiveness. Various Na-alginate concentrations (1%, 1.25%, 1.5%) were tested, with stability assessments at pH 6-9 and temperatures of 30-60 °C, alongside reusability, morphology, and amoxicillin synthesis evaluations. Initial activity was 46.59 U/mg, with optimal immobilization at 1.5% Na-alginate achieving 41.01 U/mg. After four uses, immobilized PGA BD1 retained ±20% activity with optimal conditions at pH 7 and 40 °C. Enhanced amoxicillin synthesis compared to free enzymes highlights its industrial potential. This research demonstrates the feasibility of using immobilized PGA BD1 for scaling up amoxicillin production, offering significant economic and technological benefits.
Effects of Transglutaminase on the Gel Properties of Indonesian Catfish Surimi Using Response Surface Methodology Royanti, Ida; Nandyawati, Dewi; Putri, Renny Primasari Gustia; Kusumasmarawati, Ambar Dwi; Abidin, Kharis Yohan; Pradiva, Molina Indah; Dewi, Rizky Aulia Prasasti; Gebrina, Amanda Dwi; Purwoto, Heri; Widyasti, Erma
Squalen, Buletin Pascapanen dan Bioteknologi Kelautan dan Perikanan Vol 20, No 2 (2025): August 2025
Publisher : :Agency for Marine and Fisheries Research and Human Resources, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15578/squalen.1027

Abstract

Surimi is a myofibrillar fish protein, extracted mainly from marine fish, which is commonly used to produce fish balls, crab imitation products, and various other seafood substitutes. However, finding an alternative fish from freshwater, such as freshwater catfish, is important, although its drawbacks include low gel strength and water-holding capacity. To address this problem, transglutaminase addition can maintain the surimi quality. This study aimed to improve catfish surimi characteristics by optimizing surimi production with various transglutaminase concentrations and incubation times. It used Response Surface Methodology (RSM) with Central Composite Design (CCD) to evaluate the effect of Enzyme Concentration and Incubation Time. The result showed that the catfish surimi gel strength, chewiness, whiteness, and water-holding capacity were respectively 927.513 g.cm, 3,747.18 g, 79.95 %, and 91.37 %. It was obtained by the optimum condition of surimi production with the addition of 0.85 % w/w transglutaminase and an incubation time of 36 minutes. The overall study provides insight for surimi producers to maintain surimi characteristics from freshwater fish, such as catfish.
Co-Authors Catur Sriherwanto, Catur Dewi, Rizky Aulia Prasasti Dianursanti Gebrina, Amanda Dwi Hasanah, Nuur F. Kharis Yohan Abidin, Kharis Yohan Kusumasmarawati, Ambar Dwi Pradiva, Molina Indah Purwoto, Heri Putra, Noorendra L. Putri, Renny Primasari Gustia Rahayu, Maya D. Royanti, Ida Sativa, Rizka G. Siswa Setyahadi Susi Kusumaningrum Widyasti, Erma Widyasti, Erma Widyasti