scholarly journals Isolation of Corncob Xylan-Degrading Fungi and Its Application in Xylobiose Production

Author(s):  
Tantry Febrinasari ◽  
Hasegawa Tae ◽  
Nakanishi Riki ◽  
Akkharapimon Yotsombat ◽  
Takata Goro ◽  
...  

In the present study, a potential corncob xylan degradation fungi was isolated and screened from soil to produce xylanase, and was identified as Fusarium oxysporum. The production of xylanase by F. oxysporum under solid state fermentation using corncob powder as the solid substrate reached the maximum xylanase activity when using particle size of substrate of 60 mesh, water content ratio of 2 mL/g substrate, incubation temperature of 30°C, initial pH of 6.0, size of inoculum of 5x107 spore/3 g substrate, and incubation time of 2 days. The xylanase activity increased about 4 times up to 7.92 U/mL after optimization. The potential application of xylanase of F. oxysporum in hydrolyzing alkali-treated corncob xylan to produce xylobiose was also demonstrated. Hydrolysis of 6% of corncob xylan using 100 U/g substrate of enzyme loading under optimum pH and temperature conditions (pH 5.5 and 50°C, respectively) achieved the yield of xylobiose up to 28.7 g/100 g pure xylan after 12 h incubation. The purification of hydrolysate could retain 91.1% of xylobiose. Further separation step using activated charcoal column chromatography was able to get a pure xylobiose, but could only recover 59.3% of xylobiose.

1977 ◽  
Vol 75 (2) ◽  
pp. 235-243 ◽  
Author(s):  
J. P. RENSTON ◽  
T. J. IHRIG ◽  
R. H. RENSTON ◽  
B. GONDOS ◽  
R. J. MORIN

The characteristics and localization of a cholesterol ester hydrolase enzyme in homogenates of whole testis and in isolated seminiferous tubules and interstitial cells of mature rats have been investigated. Hydrolysis of cholesteryl [1-14C]oleate occurred at an optimum pH of 7·0 was linearly related to time up to 5–6 h of incubation and increased linearly up to 0·25 mg protein/incubation. Hydrolytic activity was inhibited by increasing the incubation temperature from 29 to 41 °C and by sonication. Cholesterol ester hydrolase activity/mg protein was three times greater in homogenates of seminiferous tubules than in interstitial cells. Cholesterol ester hydrolase may function to provide precursors for use in seminiferous tubular steroid hormone biosynthesis or germ cell maturation.


2018 ◽  
Vol 6 (2) ◽  
pp. 115
Author(s):  
I Gede Yogi Wikrama Yuda ◽  
I Made Mahaputra Wijaya ◽  
Ni Putu Suwariani

The aims of this study were to determine the optimum pH of media and substrate concentration on fermentation process that affected the production of bioetanol from kluwih (Actinocarpus communis) seed by Saccharomyces cerevisiae, and to obtain initial pH of media and substrate concentration on fermentation process that can a obtain the highest concentration of bioethanol. The research was designed by 2 factors. The first factor is initial pH of media that consist of three levels: 4, 4.5, and 5. The second factor is substrate concentration that consist of three levels: 2.5 %, 5 %, and 7.5 %. The data was obtained from series of tests and then it analyzed and produced presented by descriptive method. The results showed that the initial pH of media had an effect on ethanol content, and the pH, but not effected on total resulting suspended solid. Substrate concentration had an effect on ethanol content and total suspended solid. Interaction of both treatments had an effect on ethanol content from fermented flour of kluwih seed by used Saccharomyces cerevisiae. The best treatment to produce ethanol from fermented flour of  kluwih seed is by using the initial pH of media 4.5 and substrate concentration amount 7.5 % that yielded the highest ethanol content of 6.13 mL.                                                                                                                                           Key words:  Actinocarpus communis, ethanol, fermentation, the initial pH of media, substrate concentration


2014 ◽  
Vol 508 ◽  
pp. 279-285
Author(s):  
Qi Li ◽  
Li Ya Xi ◽  
Yi Yang Feng ◽  
Lin Guo Zhao ◽  
Fei Li

The optimization of xylanase expression by recombinant Pichia pastoris were carried out in this study. Several factors were evaluated and the conclusion were as follow: the optimal conditions were in shake flask cultivation with the rotate speed 180 r/min using BMGY medium with initial pH 7.0, initial OD600 1.0, 0.1% histidine, 0.05% tween80. 1.0% methanol was added into the culture every 24 h. The xylanase activity was up to 1527 U/mL at the optimal conditions after 15 days. The optimum pH and temperature were pH5.0 and 50°C. The recombinant xylanase was stable over a pH range of 2.0-8.0. The optimal conditions of degradation were as below: after 20 h, with the pH 5.0 and temperature 45°C, 2.0% of substrate concentration, 100 U/mL of enzyme dosage and 0.05% of tween80 concentration,the degradation of xylan was the best, which indicating great potential in the bioconversion of lignocellulosic waste to xylooligosaccharide.


2009 ◽  
Vol 2009 ◽  
pp. 1-8 ◽  
Author(s):  
Eleni Gomes ◽  
Rodrigo Simões Ribeiro Leite ◽  
Roberto da Silva ◽  
Dênis Silva

An exo-PG obtained fromPenicillium viridicatumin submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme was 92 kDa, optimum pH and temperature for activity were pH 5 and 50–55∘C. The exo-PG showed a profile of an exo-polygalacturonase, releasing galacturonic acid by hydrolysis of pectin with a high degree of esterification (D.E.). IonsCa2+enhanced the stability of enzyme and its activity by 30%. TheKmwas 1.30 in absence ofCa2+and 1.16 mgmL−1in presence of this ion. In relation to theVmaxthe presence of this ion increased from 1.76 to 2.07 μmolmin−1mg−1.


2020 ◽  
Vol 13 (2) ◽  
pp. 228-241
Author(s):  
Ika Rahmatul Layly ◽  
Erma Widyasti ◽  
Deden Rosid Waltam ◽  
Ayi Mufti ◽  
Nita Wiguna ◽  
...  

AbstrakLipase adalah kelompok enzim yang mengkatalisis hidrolisis rantai panjang trigliserida, lemak, dan minyak menjadi gliserol dan asam lemak dengan adanya air. Sumber lipase untuk industri kebanyakan berasal dari mikroorganisme. Penggunaan lipase pada industri makin meningkat setiap tahunnya meliputi aplikasinya pada industri makanan, pakan, farmasi, pulp, dan kertas, biodiesel, dan industri tekstil. Dalam usaha mendapatkan isolat potensial penghasil lipase untuk hHidrofilisasi serat poliester, pada penelitian ini dilakukan skrining dan isolasi mikroorganisme yang dapat menghasilkan lipase dari limbah pengolahan minyak kelapa sawit di Malinping, Lebak, Banten. Sebanyak 20 isolat bakteri dan 5 isolat jamur yang diperoleh kemudian diuji aktivitas lipasenya menggunakan metode titrasi. Empat isolat bakteri terpilih (Kondensat, Lumpur-Got, Hasil-Buangan, dan Tangki-Crude-Oil) serta lima isolat jamur (Nut-A, Nut-B, Nut-C, Kernel-B, dan Kernel-C) dikarakterisasi pH dan suhu optimum enzimnya. Hasil karakterisasi pH menunjukkan bahwa isolat bakteri Kondensat, Lumpur-Got, Hasil-Buangan, dan Tangki-Crude-Oil mempunyai aktivitas enzim lipase tertinggi pada pH 6. Suhu optimal aktivitas enzim lipase isolat Lumpur-Got-B, Hasil Buangan-B, dan Tangki-Crude-Oil B  pada 40 °°C, sedangkan isolat bakteri-Kondensat-B optimal pada suhu 30 °°C. Aktivitas lipase kelima isolat jamur optimal pada pH 6. Suhu optimal aktivitas lipase isolat jamur Nut-A adalah 40 °°C, sedangkan isolat Nut-B, Nut-C, Kernel-B, dan Kernel-C aktivitasnya optimal pada 50 °°C.Abstract Lipase are enzymes that catalyzed the hydrolysis of triglyceride, fats and oils into glycerol and fatty acids in the presence of water. Industrial Lipase source mostly derived from microbes. Each year, the lipase utilization in industry increased, such as application for foods, feeds, pharmacys, pulp and papers, biodiesel, and textile industries. On this study, a total of 20 bacteria and 5 fungi lipase potential producer were screened and isolated from oil palm processing waste in Malinping, Lebak, Banten, which then tested for its activity using titration method. Selected isolates then were characterized for its enzyme optimum pH and temperature. The optimum pH for isolate Kondensat, Lumpur-Got, Hasil-Buangan and Crude-Oil-Tank lipases are at pH 6, whilst the optimum temperature of isolates Lumpur-Got B, Hasil-Buangan B and Crude-Oil-Tank B were at 40 °°C and bakteri-Kondensat B isolate optimum at 30 °°C. The five fungi characterization shown optimum pH at 6 and 50 °°C except for isolate Nut-A that optimum at 30 °°C.


2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Gastón Ezequiel Ortiz ◽  
Diego Gabriel Noseda ◽  
María Clara Ponce Mora ◽  
Matías Nicolás Recupero ◽  
Martín Blasco ◽  
...  

A comparative study of the proteolytic enzymes production using twelve Aspergillus strains previously unused for this purpose was performed by solid state fermentation. A semiquantitative and quantitative evaluation of proteolytic activity were carried out using crude enzymatic extracts obtained from the fermentation cultures, finding seven strains with high and intermediate level of protease activity. Biochemical, thermodynamics, and kinetics features such as optimum pH and temperature values, thermal stability, activation energy (Ea), quotient energy (Q10), Km, and Vmax were studied in four enzymatic extracts from the selected strains that showed the highest productivity. Additionally, these strains were evaluated by zymogram analysis obtaining protease profiles with a wide range of molecular weight for each sample. From these four strains with the highest productivity, the proteolytic extract of A. sojae ATCC 20235 was shown to be an appropriate biocatalyst for hydrolysis of casein and gelatin substrates, increasing its antioxidant activities in 35% and 125%, respectively.


1993 ◽  
Vol 60 (2) ◽  
pp. 229-237 ◽  
Author(s):  
Haruto Kumura ◽  
Katsuhiko Mikawa ◽  
Zenichi Saito

SummaryThe extracellular proteinase fromPseudomonas fluorescensNo. 33 was purified to electrophoretic homogeneity by a procedure including precipitation with HC1 and (NH4)2SO4, and column chromatography. The enzyme was purified 170-fold giving a yield of 7 % of the original activity. The molecular mass of the purified enzyme was 48000 by SDS-PAGE. The optimum pH and temperature for the hydrolysis of casein were 8·0–9·8 and 30–35 °C respectively. The enzyme was more thermostable in synthetic milk salts solution than in 0·1 M-sodium phosphate buffer, but was heat-labile at 50 °C in both buffer Systems. The activity was inhibited byo−phenanthroline, Hg2+, Cu2+, Fe2+and, to a lesser extent, Ni2+. Caseins were susceptible to the proteinase, but degradation patterns were dependent on the form of the casein.


Water ◽  
2021 ◽  
Vol 13 (15) ◽  
pp. 2031
Author(s):  
Ruben Miranda ◽  
Isabel Latour ◽  
Angeles Blanco

Effluent reuse is a common practice for sustainable industrial water use. Salt removal is usually carried out by a combination of membrane processes with a final reverse osmosis (RO). However, the presence of silica limits the RO efficiency due to its high scaling potential and the difficulty of cleaning the fouled membranes. Silica adsorption has many advantages compared to coagulation and precipitation at high pHs: pH adjustment is not necessary, the conductivity of treated waters is not increased, and there is no sludge generation. Therefore, this study investigates the feasibility of using pseudoboehmite and its calcination product (γ-Al2O3) for silica adsorption from a paper mill effluent. The effect of sorbent dosage, pH, and temperature, including both equilibrium and kinetics studies, were studied. γ-Al2O3 was clearly more efficient than pseudoboehmite, with optimal dosages around 2.5–5 g/L vs. 7.5–15 g/L. The optimum pH is around 8.5–10, which fits well with the initial pH of the effluent. The kinetics of silica adsorption is fast, especially at high dosages and temperatures: 80–90% of the removable silica is removed in 1 h. At these conditions, silica removal is around 75–85% (<50 mg/L SiO2 in the treated water).


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Soon Yeol Kwon ◽  
EunJu Ra ◽  
Dong Geon Jung ◽  
Seong Ho Kong

AbstractThe electrochemical activity of catalysts strongly depends on the uniform distribution of monodisperse Pt nanoparticles without aggregates. Here, we propose a new hydrolysis-assisted smearing method for Pt loading on a free-standing paper-type electrode. Polyacrylonitrile (PAN)-based nanofiber paper was used as the electrode, and it acted as a Pt support. Hydrolysis of the electrode tripled the number of active nucleation sites for Pt adsorption on the PAN nanofibers, thereby significantly enhancing the wettability of the nanofibers. This facilitated the uniform distribution of Pt nanoparticles without aggregate formation up to 40 wt% (about 0.8 mg/cm2) with a particle size of about 3 nm. The catalytic current of the hydrolyzed Pt electrode in CH3OH/H2SO4 solution exceeded 213 mA/cm2 Pt mg, which was considerably greater than the current was 148 mA/cm2 Pt mg for an unhydrolyzed electrode.


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