scholarly journals ISOLASI DAN SELEKSI KHAMIR AMILOLITIK ASAL BUAH NANGKA (Artocarpus heterophyllus Lam.)

Jurnal BIOMA ◽  
2018 ◽  
Vol 13 (1) ◽  
pp. 37-42 ◽  
Author(s):  
Tria Putri Wulandari ◽  
Dalia Sukmawati ◽  
Tri Handayani Kurniati

The aim of this research is to find the isolates of yeast that have the ability to produce enzyme amylase. The strains that can produce the amylase enzyme are characterized by a clear zone around colonies after addition of iodine solution in medium containing 1% starch soluble. Activity of amylase enzyme can be determined by measuring using spectrophotometer at λ 540 nm. The isolation result obtained 75 representative yeast isolates with colony color white butyrous 16%, white mucoid 29.3%, yellowish white 18.7%, cream 20%, peach mucoid 9.3%, and orange mucoid 6,7%. Screening results showed that 8 isolates were able to produce an amylase enzyme with code isolates K33, K34, K36, K37, K48, K107, and K128. A total of two potential yeast isolates in yielding amylase with K34 and K39 isolate codes had amylolytic index 2.89 and 2.27. The highest enzyme activity was produced by K48 (0.88 U/mL).

2018 ◽  
Vol 6 (2) ◽  
pp. 47-52
Author(s):  
Suprapto Surapto ◽  
Tri Gunaedi ◽  
Basa T. Rumahorbo

The study about the activity of the enzyme amylase from amylolytic bacterial isolates from wet sagoo starch and  its traditional provision environment had been done in Jayapura. The purposes of this study were to determine the activity of amylase enzyme and to identify the bacteria isolated from wet sagoo starch and its processing environment in Jayapura district. The method used was an experimental laboratorium in which isolation of amylolytic bacteria was performed by using nutrient agar medium with 1% soluble starch on spreed pour plate method. The enzyme activity was detected with 0.2% iodine in 2% potassium iodide which were able to form a clear zone. The protein content of the crude enzyme extract was determined by the Bradford method using bovine serum albumin (BSA). Amylase enzyme activity was determined by the formula: DUN/ml = [(R0-R1)/R0] [dilution factor] DUN/ml (dextrinizing units per ml). The results showed that there were 15 isolates amylolytic bacteria. Four (4) bacterial isolates have amylolytic power of more than 30 mm. The amilase activity of amylolytic bacterial of all  isolates were quite high: which were 35 577, 18 903,  32 106 and 46 600 U/mg for SU4, SU13, SU23 and SU40 respectively. The identification of isolates indicated that the three isolates are members of the Bacillus cereus ATCC 14 579 types with a similarity value of 71.70% to 81.10%, and one isolate is Bacillus subtilis ATCC 6501 members with a similarity value of 94.30%. Keywords: Amylolytic bacteria, amylase activity, characterization, sago flour.


2019 ◽  
Vol 6 (2) ◽  
pp. 81-84
Author(s):  
Ahmad Ikhsanudin ◽  
Emantis Rosa ◽  
Christina Nugroho Ekowati

Cockroaches (Periplaneta americana) were the insect vectors of disease that caused adverse effects on human health. Control cockroch excessive use of insecticides can lead to residus in the environment and resistance cockroach. Therefore it was necessary to use an alternatives such as such as entomopathogenic fungal as biologycal agents. The entomopathogenic fungi penetrated via the integument of an cockroach to reach the hemocoel. Proteins were the molecules responsible for integument strength in cockroach, It was synthesis the proteases to degrading proteins. The study begins with the isolation of entomopathogenic fungi using the moist chamber method with cockroach as insect bait. Fungus that grow on cockroches are cultured and purifed on Potato Dextrose Agar (PDA) medium then identified. Identification was carried out through macroscopic observations including colony color and diameter and microscopic observations including conidia, conidiophores, hyphae, vesicles, fialids, and leg cells. The result of isolation and identification obtained as Penicillium sp. Proteases enzimatic activity tested on PDA with anlene 1%. The clear zone formed is measured to show the activity of proteases produced by Penicillium sp.


2022 ◽  
Vol 951 (1) ◽  
pp. 012113
Author(s):  
I Dewiyanti ◽  
D Darmawi ◽  
Z A Muchlisin ◽  
T Z Helmi ◽  
I I Arisa ◽  
...  

Abstract Cellulolytic bacteria is one of the beneficial bacteria that can found in mangrove ecosystem. The purposes of study were to analyse the cellulolytic index, and to analyse the cellulase activity of bacteria isolated from soil mangrove. Qualitatively, assessment of cellulase activity were carried out at the Microbiology laboratory of Fish Quarantine Station, Quality Control and Safety of Fishery Products (SKIPM) Aceh, while quantitatively was observed in microbiology laboratory, Biology Department, IPB. Assessment of qualitative cellulase activity is performed by growing the selected pure isolate on 1% CMC medium then spilled 1% congo red to test its cellulolytic potential. Cellulolytic potential was determined by clear zone performed around the colony after congo red flooded. The quantitative cellulase enzyme activity test carried out by DNS method tested on one selective isolate. There were 21 from 39 isolates showed a clear zone isolated from mangrove soil. The cellulolytic index (CI) obtained ranged from 0.07 to 0.80 classified as low cellulolytic index criteria. The cellulolytic index was higher in bacteria isolated from mangrove rehabilitated than mangrove unrehabilitated. The highest cellulase activity and specific cellulase activity of BTMD32 was at 48 hours with the value were 0.0012 U/ml, 0.077 U/mg, respectively. The result concluded that the bacteria cellulolytic isolated from mangrove soil had low cellulolytic index, low cellulase activity, and low specific cellulase activity.


2019 ◽  
Vol 5 (2) ◽  
pp. 71
Author(s):  
Fatur Rahman ◽  
Ismiati Ismiati ◽  
Arbai Nurhasanah

The activity of the digestive function of animals is influenced by the secretion of extracellular enzymes from bacteria in the digestive tract. This study aims to evaluate the distribution of bacteria producing protease enzyme, amylase and lipase from the digestive tract of pearl lobster, Panulirus ornatus. Bacterial isolates that have extracellular enzyme activity are based on their ability to form clear zones in the test media. The results showed that of 51 bacterial isolates from the digestive tract of P. ornatus, proteolytic bacteria were 27.45%, amylolytic bacteria were 23.53% and lipolytic bacteria were 21.77%. Based on bacterial dominance in the gastrointestinal segment, namely the cardiac, piloric and intestinal sections, it was dominated by amylolytic bacteria at 33.33%, proteolytic at 37.50% and lipolytic at 29.41%. The activity of proteolytic, amylolytic and lipolytic bacteria based on the highest clear zone diameter was achieved respectively by SP5 isolates of 12 mm, SK10 isolates of 21 mm and SU15 isolates of 20 mm. The three bacterial isolates were potential as probiotic aquacultur candidates


2021 ◽  
Vol 913 (1) ◽  
pp. 012041
Author(s):  
I B W Gunam ◽  
I G A Sujana ◽  
I M M Wijaya ◽  
Y Setiyo ◽  
I W W P Putra ◽  
...  

Abstract Amylase has an important role in biotechnology development and occupies an important position in the world enzyme market, as a biocatalyst in various industrial fields. This study has the goal to find microbial isolates that have the ability to produce amylase enzymes. The study was conducted in two stages, namely: 1) Isolation and selection of microbes that can produce amylase enzymes using starch as substrate, was incubated for 4-7 days at 30°C. Microbial isolates that can produce amylase enzymes are characterized by the presence of clear zones around the colony after the addition of an iodine solution of 1% in the overgrown media of microbes, 2) Test the activity of amylase enzymes using a dinitrosalicylic acid reagent test. The activity of the amylase enzyme is determined by measurement using a spectrophotometer at a wavelength of 540 nm. The sample used comprised of 7 types of ragi tape and 2 samples from cassava tape that has been fermented for 5-7 days. The results obtained in the first stage were 65 microbial isolates, 16 of which had clear zones, consisting of 7 isolates from ragi tape samples and 9 isolates from cassava tape samples. In the enzyme activity test, there are several isolates that have the potential to produce amylase enzymes, these include R5I4 (0.897 ± 0.018 U/mL), R2I5.1 (0.814 ± 0.011 U/mL), R5I3 (0.727 ± 0,042 U/mL) (derived from cassava ragi tape samples) and T2I2.2 (0.812 ± 0.013 U/mL), T2I6.1 (0.817 ± 0.010 U/mL), T2I2.1 (0.735 ± 0.023 U/mL), T1I4 (0.755 ± 0.020 U/mL) (derived from cassava tape samples). The isolate with the highest enzyme activity is the R5I4 which has the value enzyme activity of 0.897 ± 0.018 U/mL and with a fairly high or moderate category, while the lowest enzyme activity is the T1I1.1 isolate of 0.284 ± 0.020 U/mL.


1967 ◽  
Vol 22 (9) ◽  
pp. 949-955 ◽  
Author(s):  
Rolf Siepmann ◽  
Hermann Stegemann

Amylases of bacteria, barley, sweet potatoes, and white potatoes were separated by electrophoresis in polyacrylamide gels containing soluble starch. After incubation in acetate buffer and staining in iodine solution, the zones of enzyme activity remained unstained. The zones of crystalline α-amylase (bacillus subtilis) and of crude α-amylase (bacteriae) were found to be identical. The main zone of the crystalline β-amylase (lpomoea batatas) was identical with the zone of crude β-amylase (barley) and with the amylase zone of the potato (solanum tuberosum) extracts. Using 5 mm slots, 1 ng of amylase is traceable. Crystalline β-amylase yielded, in addition to the main zone, a minor zone nearer to the anode. The α-amylases had three zones of different properties.Phosphorylases were demonstrated as starch synthesizing and as starch degrading enzymes by making use of the reaction: “glycogen +glucose-1-phosphat⇌starch +phosphate”. Glycogen was polymerized into the gel to demonstrate the synthesis of starch, and incubation was carried out with glucose-1-phosphate. The starch formed was stained with iodine. The extracts of freshly harvested tubers yielded four zones, whereas those of stored tubers yielded two zones, and leaves and sprouts each showed one zone. - To observe starch degradation by phosphorylases, starch was polymerized into the polyacrylamide, and the gels were incubated in phosphate buffer. After treatment with iodine, an unstained zone was observed which corresponded to the most intense phosphorlase zone (close to the anode) in the glycogen gel. This zone was more intense in the tuber extracts than in leaves and sprouts.Pig heart extract contained the phosphorylase in the b form. Three zones have been observed. - Extracts of rat muscle and heart yielded phosphorylases which corresponded in their migration rate and in their requirement for adenosine-5′-monophosphate to the b form of pig heart phosphorylase. The same was true for the migration rate of liver phosphorylase.Crystalline α-phosphorylase of rabbit muscle required the addition of cystein to the electrophoresis buffer during separation. Two zones of activity could be demonstrated.


Author(s):  
S.M. Geyer ◽  
C.L. Mendenhall ◽  
J.T. Hung ◽  
E.L. Cardell ◽  
R.L. Drake ◽  
...  

Thirty-three mature male Holtzman rats were randomly placed in 3 treatment groups: Controls (C); Ethanolics (E); and Wine drinkers (W). The animals were fed synthetic diets (Lieber type) with ethanol or wine substituted isocalorically for carbohydrates in the diet of E and W groups, respectively. W received a volume of wine which provided the same gram quantity of alcohol consumed by E. The animals were sacrificed by decapitation after 6 weeks and the livers processed for quantitative triglycerides (T3), proteins, malic enzyme activity (MEA), light microscopy (LM) and electron microscopy (EM). Morphometric analysis of randomly selected LM and EM micrographs was performed to determine organellar changes in centrilobular (CV) and periportal (PV) regions of the liver. This analysis (Table 1) showed that hepatocytes from E were larger than those in C and W groups. Smooth endoplasmic reticulum decreased in E and increased in W compared to C values.


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