Characterization of a family 3 polysaccharide lyase with broad temperature adaptability, thermo-alkali stability, and ethanol tolerance

2012 ◽  
Vol 17 (4) ◽  
pp. 729-738 ◽  
Author(s):  
Junpei Zhou ◽  
Yanyan Dong ◽  
Yajie Gao ◽  
Xianghua Tang ◽  
Junjun Li ◽  
...  
Extremophiles ◽  
2021 ◽  
Author(s):  
Xin Chang ◽  
Shuang Wu ◽  
Jie Chen ◽  
Shengqi Xiong ◽  
Peng Wang ◽  
...  

Marine Drugs ◽  
2019 ◽  
Vol 17 (12) ◽  
pp. 681
Author(s):  
Junhao Sun ◽  
Xu Han ◽  
Guanrui Song ◽  
Qianhong Gong ◽  
Wengong Yu

Glycosaminoglycan (GAG) lyase is an effective tool for the structural and functional studies of glycosaminoglycans and preparation of functional oligosaccharides. A new GAG lyase from Microbacterium sp. H14 was cloned, expressed, purified, and characterized, with a molecular weight of approximately 85.9 kDa. The deduced lyase HCLaseM belonged to the polysaccharide lyase (PL) family 8. Based on the phylogenetic tree, HCLaseM could not be classified into the existing three subfamilies of this family. HCLaseM showed almost the same enzyme activity towards hyaluronan (HA), chondroitin sulfate A (CS-A), CS-B, CS-C, and CS-D, which was different from reported GAG lyases. HCLaseM exhibited the highest activities to both HA and CS-A at its optimal temperature (35 °C) and pH (pH 7.0). HCLaseM was stable in the range of pH 5.0–8.0 and temperature below 30 °C. The enzyme activity was independent of divalent metal ions and was not obviously affected by most metal ions. HCLaseM is an endo-type enzyme yielding unsaturated disaccharides as the end products. The facilitated diffusion effect of HCLaseM is dose-dependent in animal experiments. These properties make it a candidate for further basic research and application.


Author(s):  
Danmadami ◽  
Yabaya ◽  
Yahaya O ◽  
Abraham ◽  
Bobai M ◽  
...  

Non-availability and relatively high cost of obtaining the most effective commercially alcoholic fermentative Saccharomyces cereviciae strain is a major constrain in development and sustaining local industrial fermentation process. This study determined the alcoholic fermentative efficiency of Saccharomyces cereviciae strains isolated from palm wine in the production of burukutu. Palm wine was collected from Kachia, a sub-urban area of Kaduna, Kaduna State, Nigeria. Isolation was carried out using Sabouroud dextrose agar. Identification and characterization of Saccharomyces cereviciae from palm wine was carried out by microscopy and conventional biochemical methods and Analytical Profile Index. Alcoholic fermentative efficiency of the yeasts isolates was determined through fermentation of sorghum for the production of Burukutu. Ethanol tolerance and some physiological test were conducted. Cultural and morphological characteristics revealed smooth, creamy and white colonies on SDA, while cellular morphology was round and budded in arrangement. Biochemical identification and API showed isolate that was Glucose, Galactose, Raffinose, Acetyl D glucosamine positive and Glycerol, Inositol, Sorbitol, Arabinose, D –xylose, Adonitol Xylitol, Celiobiose, 2 – Ketoglutanal, Lactose, Maltose, Tretialose, Melezitose negative. HyphoePsedudohyphae and the control carbohydrate utilized were negative. The ethanol tolerance characteristics of the yeast revealed that the isolate had 8% ethanol tolerant. The pH of the Burukutu produced with Saccharomyces cerevisiae isolated from palm wine ranged from 3.8 – 6.2, in a manner showing pH decrease from 6.2 to 3.8 Within 24 hours’ fermentation period. Volatile acidity was also observed to have reduced during the study period. The total viable yeast also increased gradually, thus showing its ability to to metabolize sugar in sorghum to produce alcohol in burukutu.


2020 ◽  
Vol 164 ◽  
pp. 3762-3770
Author(s):  
Zhelun Zhang ◽  
Hang Su ◽  
Xiaoyi Wang ◽  
Luyao Tang ◽  
Jingyang Hu ◽  
...  

1964 ◽  
Vol 42 (1) ◽  
pp. 87-93 ◽  
Author(s):  
H. Singh ◽  
B. G. Lane

Methods are described which are suitable for the quantitative analysis of the alkali-stable oligonucleotides which result from the hydrolysis of ribonucleates in molar alkali at room temperature for 90 hours. The alkali-stability of the oligonucleotides is presumed to result from 2′-O-methyl substitution of ribose residues and this assumption is supported by the relatively slight reactivity of the purine 2′-O-methyl ribosides in the orcinol color reaction for pentoses. The existence of all of the 16 possible dinucleotides as part of ribonucleate chains has been established. The quantity of alkali-stable trinucleotides is much greater than would be expected for a random spatial distribution of 2′-O-methyl ribosides in ribonucleate chains.


2018 ◽  
Vol 32 (S1) ◽  
Author(s):  
ThirumalaiSelvi Ulaganathan ◽  
William Helbert ◽  
Ehud Banin ◽  
Miroslaw Cygler

Marine Drugs ◽  
2019 ◽  
Vol 17 (10) ◽  
pp. 568 ◽  
Author(s):  
Jian Gao ◽  
Chunying Du ◽  
Yongzhou Chi ◽  
Siqi Zuo ◽  
Han Ye ◽  
...  

Ulvan lyases can degrade ulvan to oligosaccharides with potent biological activity. A new ulvan lyase gene, ALT3695, was identified in Alteromonas sp. A321. Soluble expression of ALT3695 was achieved in Escherichia coli BL21 (DE3). The 1314-bp gene encoded a protein with 437 amino acid residues. The amino acid sequence of ALT3695 exhibited low sequence identity with polysaccharide lyase family 25 (PL25) ulvan lyases from Pseudoalteromonas sp. PLSV (64.14% identity), Alteromonas sp. LOR (62.68% identity), and Nonlabens ulvanivorans PLR (57.37% identity). Recombinant ALT3695 was purified and the apparent molecular weight was about 53 kDa, which is different from that of other polysaccharide-degrading enzymes identified in Alteromonas sp. A321. ALT3695 exhibited maximal activity in 50 mM Tris-HCl buffer at pH 8.0 and 50 °C. ALT3695 was relatively thermostable, as 90% activity was observed after incubation at 40 °C for 3 h. The Km and Vmax values of ALT3695 towards ulvan were 0.43 mg·mL−1 and 0.11 μmol·min−1·mL−1, respectively. ESI-MS analysis showed that enzymatic products were mainly disaccharides and tetrasaccharides. This study reports a new PL25 family ulvan lyase, ALT3695, with properties that suggest its great potential for the preparation of ulvan oligosaccharides.


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