Newly Isolated Penicillium ramulosum N1 Is Excellent for Producing Protease-Resistant Acidophilic Xylanase

2015 ◽  
Vol 25 (5) ◽  
pp. 320-326 ◽  
Author(s):  
Chaoyang Lin ◽  
Zhicheng Shen ◽  
Tingheng Zhu ◽  
Wensheng Qin

<i>Penicillium ramulosum</i> N1 was isolated from decaying wood. This strain produces extracellular xylanases and cellulases. The highest activities of xylanases (250 U/ml) and carboxymethyl cellulose (CMCase; 6.5 U/ml) were produced when 1% barley straw was added as a carbon source. The optimum temperature and pH for xylanase activity was 55 and 3.0°C, respectively. The xylanases exhibited strong protease resistance. CMCase revealed maximum activities at pH 3.0 and in the range of 60-70°C. Filter paper activity was optimally active at pH 5.0 and 55°C. The zymograms produced by the SDS-PAGE resolution of the crude enzymes indicated that there are four bands of protein with xylanase activity and three bands of proteins with endoglucanase. The results revealed that <i>P. ramulosum</i> N1 is a promising acidophilic and protease-resistant xylanase-producing microorganism that has great potential to be used in animal feed and food industry applications.

Gold Bulletin ◽  
2021 ◽  
Author(s):  
Saeed Paidari ◽  
Salam Adnan Ibrahim

AbstractIn the past few decades, there have been remarkable advances in our knowledge of gold nanoparticles (AuNPs) and synthesizing methods. AuNPs have become increasingly important in biomedical and industrial applications. As a newly implemented method, AuNPs are being used in nanopackaging industries for their therapeutic and antibacterial characteristics as well as their inert and nontoxic nature. As with other NPs, AuNPs have privileges and disadvantages when utilized in the food sector, yet a significant body of research has shown that, due to the specific nontoxic characteristics, AuNPs could be used to address other NP flaws. In this mini review, we present synthesizing methods, food industry applications, and mechanisms of action of gold nanoparticles. Regarding the investigations, gold nanoparticles can play a major role to reduce microbial load in foodstuff and therefore can be implemented in food packaging as an effective approach.


Author(s):  
Ornella M Ontañon ◽  
Soma Bedő ◽  
Silvina Ghio ◽  
Mercedes M Garrido ◽  
Juliana Topalian ◽  
...  

Abstract One of the main distinguishing features of bacteria belonging to the Cellulomonas genus is their ability to secrete multiple polysaccharide degrading enzymes. However, their application in biomass deconstruction still constitutes a challenge. We addressed the optimisation of the xylanolytic activities in extracellular enzymatic extracts of Cellulomonas sp. B6 and Cellulomonas fimi B-402 for their subsequent application in lignocellulosic biomass hydrolysis by culture in several substrates. As demonstrated by secretomic profiling, wheat bran and waste paper resulted to be suitable inducers for the secretion of xylanases of Cellulomonas sp. B6 and C. fimi B-402, respectively. Both strains showed high xylanolytic activity in culture supernatant although Cellulomonas sp. B6 was the most efficient xylanolytic strain. Upscaling from flasks to fermentation in a bench scale bioreactor resulted in equivalent production of extracellular xylanolytic enzymatic extracts and freeze drying was a successful method for concentration and conservation of the extracellular enzymes, retaining 80% activity. Moreover, enzymatic cocktails composed of combined extra and intracellular extracts effectively hydrolysed the hemicellulose fraction of extruded barley straw into xylose and xylooligosaccharides. Key points • Secreted xylanase activity of Cellulomonas sp. B6 and C. fimi was maximised. • Biomass-induced extracellular enzymes were identified by proteomic profiling. • Combinations of extra and intracellular extracts were used for barley straw hydrolysis.


2013 ◽  
Vol 59 (No. 3) ◽  
pp. 98-104 ◽  
Author(s):  
P. Vaculík ◽  
J. Maloun ◽  
L. Chládek ◽  
M. Přikryl

Grinding or crushing hard raw materials is usually a primary operation which precedes the follow-up technological processes in a number of industrial sectors. A great variety of machines using different principles of fragmentation are employed in the technology of pulverization. The food industry uses roller mills, in which the main process is the shear grinding. In the animal feed industry impact machines known as hammer mills are often used. In recent years, mills have been employed that use their frontal edges for grinding or crushing during the rotation of one of two adjacent discs. The modern design disc machines used for grinding grain have resulted from long development and their operation has a relatively low noise level with reduced dust. The separation process that occurs in the gap between the active edges of the discs can be described as shear grinding and is currently the subject of attention which is focused on the specific energy consumption and fractional composition of the product of grinding. &nbsp;


2017 ◽  
Vol 3 (5) ◽  
pp. 139
Author(s):  
Mariana Wahjudi ◽  
Catherina . ◽  
Nita Marcelia Wangunhardjo ◽  
Ernest Suryadjaja ◽  
Xavier Daniel

<p class="Els-Abstract-text">The <em>xyn</em>B gene of <em>Bacillus</em><em> subtilis</em> subsp. spizizenii W23 is predicted to encode a xylan 1,4-beta-xylosidase. Application of XynB enzymes in industries is wide. Production of this enzyme in its host cells is naturally restricted by repression process. It will give certain beneficial to over-expressed the enzymes in other host-cells under inducing promoter. This study aimed to clone the <em>xyn</em>B gene from <em>Bacillus</em><em> subtilis</em> subsp. spizizenii W23, to pMMB67EH plasmid, and to over-express the <em>xyn</em>B gene in <em>Escherichia coli </em>Origami as host cells. The <em>x</em><em>yn</em>B gene was successfully amplified by polymerase chain reaction (PCR) technique using a pair of primers flanking the gene sequence and chromosomal DNA of the W23 strain as a template. The <em>xyn</em>B gene inserted in recombinant plasmid was confirmed by PCR detection using primers pair’s specific for <em>xyn</em>B gene and for the vector, then continued by restriction analyses.  The result showed that transformants clone 9 and 10 bear the recombinant pMMB-<em>xyn</em>B plasmid. The xylanase activity of <em>xyn</em>B gene in <em>Escherichia coli</em> Origami clone 10 was detected by sodium-dodecyl-sulfate polyacrylamide gel analyses and with addition of isopropyl-β-D-thio-galactoside (IPTG) as an inducer. The protein seem to be over-expressed as intra- and extra-cellular protein detected on SDS-PAGE gel. Result from xylan degrading activity on Luria-Bertani-xylan-IPTG plate with addition of Congo Red, showed that the cells with pMMB-<em>xyn</em>B recombinant plasmid have clear zone around the colonies while the transformant bearing an empty plasmid showed no clear zone. It could be concluded that the <em>xyn</em>B gene of <em>Bacillus subtilis</em> subsp.spizizenii W23 has been successfully been cloned on pMMB67EH plasmid and over-expressed in the <em>Escherichia coli</em> Origami cells as intra- and extra-cellular protein, as observed on SDS-PAGE gel analysis. The protein has activity on xylan degradation.</p>


2010 ◽  
Vol 10 (2) ◽  
pp. 256-260 ◽  
Author(s):  
Hasnah Natsir ◽  
Abd. Rauf Patong ◽  
Maggy Thenawidjaja Suhartono ◽  
Ahyar Ahmad

Chitinase is an extracellular enzyme which is capable in hydrolyzing insoluble chitin to its oligomeric and monomeric components. The enzyme produced by thermophilic bacteria was screened and isolated from Sulili hot spring in Pinrang, South Sulawesi, Indonesia. The gram positive spore forming rod shape bacteria was identified as Bacillus sp. HSA,3-1a through morphological and physiological analysis. The production of chitinase enzyme was conducted at various concentration of colloidal chitin at a pH of 7.0 and a temperature of 55 °C. The bacteria optimally was produced the enzyme at a colloidal chitin concentration of 0.5% after 72 h of incubation. The optimum temperature, pH and substrate concentration of chitinase were 60 °C, 7.0 and 0.3%, respectively. The enzyme was stable at a pH of 7.0 and a temperature of 60 °C after 2 h of incubation. The chitinase activities was increased by addition of 1 mM Mg2+, Ca2+ and Mn2+ ions, whereas the activities were  decreased by 1 mM Co2+, Fe2+ and Zn2 ions. The molecular weight of the crude enzyme was determined using SDS-PAGE analysis. Five protein fractions were obtained from SDS-PAGE, with MWs of 79, 71, 48, 43 and 22 kDa.   Keywords: colloidal chitin, thermophilic bacteria, chitinase


1999 ◽  
Vol 181 (1) ◽  
pp. 91-99 ◽  
Author(s):  
Hisayo Ono ◽  
Kazuhisa Sawada ◽  
Nonpanga Khunajakr ◽  
Tao Tao ◽  
Mihoko Yamamoto ◽  
...  

ABSTRACT 1,4,5,6-Tetrahydro-2-methyl-4-pyrimidinecarboxylic acid (ectoine) is an excellent osmoprotectant. The biosynthetic pathway of ectoine from aspartic β-semialdehyde (ASA), in Halomonas elongata, was elucidated by purification and characterization of each enzyme involved. 2,4-Diaminobutyrate (DABA) aminotransferase catalyzed reversively the first step of the pathway, conversion of ASA to DABA by transamination with l-glutamate. This enzyme required pyridoxal 5′-phosphate and potassium ions for its activity and stability. The gel filtration estimated an apparent molecular mass of 260 kDa, whereas molecular mass measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was 44 kDa. This enzyme exhibited an optimum pH of 8.6 and an optimum temperature of 25°C and had Km s of 9.1 mM forl-glutamate and 4.5 mM for dl-ASA. DABA acetyltransferase catalyzed acetylation of DABA to γ-N-acetyl-α,γ-diaminobutyric acid (ADABA) with acetyl coenzyme A and exhibited an optimum pH of 8.2 and an optimum temperature of 20°C in the presence of 0.4 M NaCl. The molecular mass was 45 kDa by gel filtration. Ectoine synthase catalyzed circularization of ADABA to ectoine and exhibited an optimum pH of 8.5 to 9.0 and an optimum temperature of 15°C in the presence of 0.5 M NaCl. This enzyme had an apparent molecular mass of 19 kDa by SDS-PAGE and a Km of 8.4 mM in the presence of 0.77 M NaCl. DABA acetyltransferase and ectoine synthase were stabilized in the presence of NaCl (>2 M) and DABA (100 mM) at temperatures below 30°C.


Author(s):  
A.S. Volkova ◽  
◽  
A.A. Mnatsakanyan ◽  
G.V. Chuvarleeva ◽  
◽  
...  

This article indicates the results of studies of the effect of various doses of mineral fertilizers with trace elements based on pure silicon – “Nanosilicon” – on the productivity of soybean plants. Soya is a unique crop in its specificity. It is widely used in the food industry, both in the process of human food production, and in the production of animal feed. Silicon is the second most abundant element in the lithosphere of our planet. It increases stress resistance of plants, improves absorbing capacity of the root system, helps plants to retain moisture in the dry period, and strengthens the cell walls of plants. In general, the result was positive regardless of the amount of the preparation used, so the yield increased on average by 12.9 %, oil collection – by 12.8 %, and protein collection – by 15.1 %.


2018 ◽  
Vol 22 ◽  
pp. 28-42 ◽  
Author(s):  
Christos Soukoulis ◽  
Claire Gaiani ◽  
Lucien Hoffmann

2020 ◽  
Vol 9 (5) ◽  
pp. 173-184
Author(s):  
Fatima Zohra Baghdad Belhadj ◽  
Faiza Boublenza ◽  
Nour-Eddine Karam

Lactobacillus plantarum is a lactic acid bacterium widely used in the food industry because of its beneficial effects on human health and its ability of adaptation to different stress conditions, hence the purpose of this work was to study the adaptation abilities of Lactobacillus plantarum LM6 and stress proteins involved during this adapta on. Lb. plantarum LMF6 was isolated from human breast milk and was exposed to acid, alkaline, thermal, oxidative, osmotic, detergent and nutritional stresses in order to determine their effects on growth, viability, tolerance and mortality. SDS-PAGE electrophoresis allowed us to compare the total proteins in the absence and in the presence of stress then the ImageJ® so ware analyzed the obtained pro les. The results show that Lb. plantarum LMF6 is highly tolerant to osmo c (at 9% NaCl, the UFC number is 3.4×1010 UFC/ml), alkaline (4.7×107UFC/ml at pH10), detergent (the UFC number is close to the control), oxydative (3.3×108 UFC/ml), nutri onnal (5.2×107 UFC/ml), acid (pH5, pH4 and pH3) and heat (40°C, 45°C and 50°C with 1.45×1011, 2.78×109 and 2.80×108UFC/ml respec vely) stresses, but sensi ve to extreme acid stress (pH1 and pH2 with mortality rate variable from 5log to 10log) and extreme heat stress (55°C and 60°C when mortality increases to 8log at 60°C). Comparison of proteins profiles allowed us to see quantitative and qualitative differences. Our results allowed to say that Lb. plantarum LMF6 showed interesting characteristics and could be used in food industry as probio c lactobacilli.


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