Budiasih Wahyuntari
Laboratoria Pengembangan Teknologi Industri Agro-Biomedika (LAPTIAB), Badan Pengkajian dan Penerapan Teknologi, Kawasan Pusat Teknologi dan Ilmu Pengetahuan (PUSPIPTEK) gedung no 610, Serpong, Tangerang 15310

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ISOLATION of a AMYLASE INHIBITORS from MUNGBEAN and SOYBEAN and INHIBITORY EFFECT on HUMAN SALIVARY and PORCINE PANCREATIC AMYLASE wahyuntari, budiasih; Tekol, Martinus Nicoadi Tekol
Jurnal Sains dan Teknologi Indonesia Vol. 14 No. 1 (2012)
Publisher : Badan Pengkajian dan Penerapan Teknologi

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (750.133 KB) | DOI: 10.29122/jsti.v14i1.899

Abstract

Penghambat alfa amilase adalah salah satu komponen dalam suplemen makanan yang telah lama digunakan untuk terapi kegemukan karena penghambat amilase mempengaruhi metabolisme karbohidrat dalam sistem pencernaan. Sejumlah peneliti melaporkan terdapat dua grup penghambat amilase, yaitu protein dan non protein. Penghambat protein dilaporkan terdapat dalam kelompok kacang-kacangan dan biji-bijian. Tujuan penelitian ini adalah untuk mengisolasi penghambat protein yang terdapat dalam kacang hijau dan kedele. Kacang hijau dan kedele merupakan kacang-kacangan yang penting dalam makanan popular di Indonesia. Penghambat protein diendapkan dengan konsentrasi bertingkat garam ammonium sulfat [(NH)4SO4] dari 30-70%. Penghambat protein diuji terhadap amilase saliva manusia (HSA) danamilase pankreas babi (PPA), serta kestabilannya terhadap pemanasan pada 100oC selama 30 menit. Hasil penelitian menunjukkan bahwa semua endapan jenuh dari semua konsentrasi amonium sulfat yang diuji menghambat PPA, tetapi tidak semua endapan jenuh tersebut dapatmenghambat HSA. Hanya semua endapan jenuh (NH)4SO4 dari kacang hijau yang dapat menghambat HSA, dan penghambatan tertinggi terhadap HSA adalah endapan jenuh (NH)4SO4 50%. Endapan jenuh (NH)4SO4 40 % dari kedele putih dan endapan jenuh (NH)4SO4 60% dari kedele hitam dengan masing-masing penghambatan 98.67; 26.86 and27.63%. Endapan jenuh (NH)4SO4 60-70% dari kacang hijau, 50% dari kedele putih dan 50% dari kedele hitam menghambat PPA 100%. Pemanasan penghambat pada 100oC selama 30 menit hampir tidak mempengaruhi penghambatannya terhadap PPA. Profil protein juga diamati menggunakan analisis SDS/PAGE.
PEMANFAATAN BERBAGAI JENIS PATI SEBAGAI SUMBER KARBON UNTUK PRODUKSI a-AMILASE EKSTRASELULER Bacillus sp SW2 Trismilah, Trismilah; Wahyuntari, Budiasih
Jurnal Sains dan Teknologi Indonesia Vol. 11 No. 3 (2009)
Publisher : Badan Pengkajian dan Penerapan Teknologi

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (178.763 KB) | DOI: 10.29122/jsti.v11i3.841

Abstract

Currently enzymes become a need of food and non-food industries. Alpha amylase (a-1,4 glucanohydrolase, EC 3.2.1.1) is an enzyme that hydrolyses starch into oligosaccharides and dextrin. The enzyme has been commercially available which mostly produced by Bacillus spp. The bacterium used in thisexperiment was Bacillus sp SW2, which was isolated from Composting Unit at Bumi Serpong Damai, Tangerang. The aim of this experiment was to find the most appropriate starch as an carbon source for enzyme production. The starches observed were tapioca, potato, and cornstarch at concentration of5%. The fermentation was conducted in shaking incubator, in 125 ml Erlenmeyer at 60°C, various pHs, and agitations. The pHs observed were 6, 7.5, 8 and 9 while the rates of agitation applied were 150, 200, and 250 rpm. The results showed that the highest enzyme activity was 20.99 Unit/ml, whichwas reached after 42 hours of fermentation using cornstarch, pH 8 and 200 rpm agitation.
Characterization of Protease from Bacillus licheniformis F11.1 as a Bio-Detergent Agent lmiah, Sitti Nur; Mubarik, Nisa Rachmania; Wahyuntari, Budiasih
Makara Journal of Science Vol. 22, No. 3
Publisher : UI Scholars Hub

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Abstract

Proteases are among the most important enzymes in both food and non-food industries taking up almost 60% of the world enzyme market. This enzyme has been used for many industrial processes, especially in the detergent industry. The purpose of this study was to characterize the protease from Bacillus licheniformis F11.1 as a bio-detergentagent. An enzyme assay of protease activity was used to assess and characterize the protease enzyme from B. licheniformis F11.1. It showed that the highest pH protease activity for alkaline protease occurred at pH 8.0 with a value of 35.00U/mL. Under incubation temperature, the protease had the highest activity at 50 °C with a value of 24.46 U/mL. Protease activity was inhibited by Ca2+,Mn2+, K+, and Na+ions at concentrations of 5 mM. Protease activity can beenhanced by these ions at concentrations of 2 mM. Protease stability can be measured from half-life. Under anincubation temperature of 50 °C, the half-life of the protease at pH 8, 9, and 10 was 108 min, 114 min, and 98 min, respectively. The assay for enzyme stability with an incubation temperature of 60 °C showed half-lives of 92 minutes, 56 minutes, and 61 minutes for pH 6, 9, and 10, respectively. This enzyme was found to be stable with the addition ofdetergent compounds such as sodium dodecyl sulfate (SDS), Triton X-100, ethylenediaminetetraacetic acid (EDTA), and hydrogen peroxide; all under low concentrations. Determination of the molecular weight using SDS-PAGE andzymogram found the molecular weight was 32.90-35.16 kDa. These results showed that the alkaline protease from B.licheniformis F11.1 can be used as a bio-detergent because of its tolerance to various detergent compounds.