Fermentasi Nira Sorgum Manis Menjadi Etanol (Alcoholic Fermentation of Sweet Sorghum Juice)

Sweet sorghum juice about 11-16% of total sugar, and so it could be potentially fermenled to produce ethanol. The concentrated juices were used as media for ethanol production in batch culture using Saccharomyces cerevisiae R5 at 30°C and pH 4.5. The ethanol yield (Yp/s ) and volumetric productivity during 48 hours of fermentation lime with 20.08%(x/v) initial sugar contents were 0.44 g.g-1 and O.18 g.1-1.h-1,respectively

Kinetic Parameters of Endochitinase From Bacillus Licheniformis MB-2

Parameter Kinetika Endokitinase dari Bacillus licheniformis MB-2. Bacilluslicheniformis MB-2 yang diisolasi dari air panas di Tompaso (Sulawesi Utara)menghasilkan 5 enzim kitinase ekstraselular. Salah satu enzim, Chi-67, telah dimumikandan diarekterisasi. Chi-67 dapat menghidrolisis substrat kitin buatan maupun alami.Analisis kinetika aktivitas enzim terhadap berbagai substrat kitin telah dilakukan. Enzimdapat memotong 4-methylumbelliferyl N', N'-diacetylchitobioside {MUF(GINAc),}, 4-methylumbellifelyl N:N' N'-triacetylchitotrioside {MUF(GINAc),), glikol kitin, dankoloidal kitin, tetapi tidak dapat melepaskan senyawa MUF dari 4-methylumbelliferylN-acetyl-R-D-glucosamine {MUF(GINAc)}. Ini menunjukkan Chi-67 memiliki tipepernotongan endo. K u ~kaec epatan reaksi substrat menunjukkan pola profil Michaelis-Menten. Kecepatan reaksi maksimum (V,,) terhadap MUF(GlNAc), identik denganVmatxe rhadap MUF(GINAC)~ya itu 0.02 pM.mitil . VmaeXn zim terhadap koloidal kitinadalah 0.01 pM.h-' atau lebih rendah 3 kali dari nilai VmaXpa da substrat glikol kitin (0.03M h ) Nilai Kcu, untuk koloidal kitin sebesar 8.01 h-' atau hampir 2 kali lebih tinggidari glikol kitin (4.32 h-I) sementara Kc, untuk MUF(GlNAc),adalah 3.65 min-' atau1,5 kali lebih tinggi dari Kc%,M UF(GINAc), yang hanya 2.90 min-' . Afinitas Chi-67terhadap koloidal kitin, glikol kitin, MUF(GINAc),, dan MUF(GINAc), yang ditunjukkanoleh nilai konstanta Michaelis (K,) masing-masing 3.08 rng.ml-I, 0.32 mg.ml-I, 0.26 mMdan 0.1 mM

Optimasi Produksi Fructosyltransferase Oleh Aspergillw SP. Wnic [the Optimization of Fructosyltransferase Production by Aspergillus SP Wnic]

Fructo Oligo Saccharides (FOS) are considered as biologically benefit, have been developed recently to be used as functional factors in healthy foods.FOS shows low cariogenicity, nondigestibility and proliferation of bifidobacteria in human intestinal tract and dietary fiberlike action. The aim of this research is to produce FOS from sucrose by using fructocyltransferase (FT-ase) from Aspergillus sp. Research on the production of FOS was the optimization of FT-ase production. Inoculum of selected Aspergillus was added into medium with various composition and incubation conditions. Enzyme solution was mixed with sucrose and incubated at various times, pHs, temperatures and agitations.The best parameter condition was based on the highest FT-ase activity. The results showed that production of FT-ase was affected by fermentation time, pH and incubation temperature. The carbon source tested permitted good growth and enzyme production where sucrose supported rather good enzyme production.It was obvious that enzyme production was not closely correlated with cell growth.The best fructo-oligosaccharide yield (20.53%) was achieved when 20 g/100 ml sucrose was utilized. Yeast extract was good nitrogen source for enzyme production. The best FT-ase activity was achieved when 1.2 g/100 ml yeast extract was utilized. Addition of mineral salt also enhanced enzyme production where 1 g/l magnesium salt gave the best cell growth and enzyme production

STUDI PENDAHULUAN ENZIM KITINASE EXTRASELULER YANG DIHASILKAN OLEH ISOLAT BAKTERI ASAL MANADO 1) [Preliminary Study of Extracellular Chitinase Produced by Bacteria Isolated from Manado]

Chitinolytic bacteria were isolated from several exotic area in Manado Province. The most potential isolate, namely 13.26, was isolated from Tompaso. The isolate was cultured in the thermus medium containing colloidal chitin as a carbon source for 5 days at 55°C to produce chitinase. It was observed that chitinase was most active at 65��C and the optimum pH was 8 in boric acid-borax buffer. Ammonium sulfate (50% saturation) precipitation of the protein increased the specific activity of the enzyme from 0.20 unit/mg protein (in culture supernatant) to 0.28 unit/mg protein. The molecular weight as estimated by zymogram analysis was180 kD

STUDI PENDAHULUAN ENZIM KITINASE EXTRASELULER YANG DIHASILKAN OLEH ISOLAT BAKTERI ASAL MANADO 1) [Preliminary Study of Extracellular Chitinase Produced by Bacteria Isolated from Manado]

Chitinolytic bacteria were isolated from several exotic area in Manado Province. The most potential isolate, namely 13.26, was isolated from Tompaso. The isolate was cultured in the thermus medium containing colloidal chitin as a carbon source for 5 days at 55°C to produce chitinase. It was observed that chitinase was most active at 65°C and the optimum pH was 8 in boric acid-borax buffer. Ammonium sulfate (50% saturation) precipitation of the protein increased the specific activity of the enzyme from 0.20 unit/mg protein (in culture supernatant) to 0.28 unit/mg protein. The molecular weight as estimated by zymogram analysis was180 kDa

STUDI PENDAHULUAN ENZIM KITINASE EXTRASELULER YANG DIHASILKAN OLEH ISOLAT BAKTERI ASAL MANADO 1) [Preliminary Study of Extracellular Chitinase Produced by Bacteria Isolated from Manado]

Chitinolytic bacteria were isolated from several exotic area in Manado Province. The most potential isolate, namely 13.26, was isolated from Tompaso. The isolate was cultured in the thermus medium containing colloidal chitin as a carbon source for 5 days at 55°C to produce chitinase. It was observed that chitinase was most active at 65°C and the optimum pH was 8 in boric acid-borax buffer. Ammonium sulfate (50% saturation) precipitation of the protein increased the specific activity of the enzyme from 0.20 unit/mg protein (in culture supernatant) to 0.28 unit/mg protein. The molecular weight as estimated by zymogram analysis was180 kDa

Purification of a thermostable chitinase from Bacillus cereus by chitin affinity and its application in microbial community changes in soil

[[abstract]]A thermostable chitinase was purified by chitin affinity from the culture supernatant of Bacillus cereus TKU028 with shrimp head powder (SHP) as the sole carbon/nitrogen source. TKU028 chitinase was purified using a one-step affinity adsorbent system, and the molecular mass of TKU028 chitinase (approximately 40 kDa) was then determined using SDS-PAGE. The enzyme was stable for 60 min at temperatures below 60 °C and stable over a broad pH range of 4–9 for 60 min. In addition, the temporal changes of a bacterial community in mangrove river sediment of the Tamsui River with added SHP were also analysed by PCR–denaturing gradient gel electrophoresis to investigate the effects of B. cereus TKU028 on the degradation of SHP. The 6-week incubation sample of SHP and B. cereus TKU028-amended mangrove river sediment displayed the highest amount of biomass, reducing sugar and total sugar, and some variance of bacterial community composition existed in the soils.[[notice]]補正完畢[[incitationindex]]SCI[[booktype]]紙