scholarly journals Production of Thermophilic Chitinase by Paenibacillus sp. TKU052 by Bioprocessing of Chitinous Fishery Wastes and Its Application in N-acetyl-D-glucosamine Production

Polymers ◽  
2021 ◽  
Vol 13 (18) ◽  
pp. 3048
Author(s):  
Chien Thang Doan ◽  
Thi Ngoc Tran ◽  
San-Lang Wang
Keyword(s):  
Enzyme Production ◽  
Production Cost ◽  
Maximum Activity ◽  
Paenibacillus Sp ◽  
Negative Effect ◽  
Chitinase Production ◽  
Tween 40 ◽  
Triton X ◽  
Catalytic Functions ◽  
Hydrolysis Of

The bioprocessing of chitinous fishery wastes (CFWs) to chitinases through fermentation approaches has gained importance owing to its great benefits in reducing the enzyme production cost, and utilizing chitin waste. In this work, our study of the chitinase production of Paenibacillus sp. TKU052 in the presence of different kinds of CFWs revealed a preference for demineralized crab shells powder (deCSP); furthermore, a 72 kDa chitinase was isolated from the 0.5% deCSP-containing medium. The Paenibacillus sp. TKU052 chitinase displayed maximum activity at 70 °C and pH 4–5, while Zn2+, Fe3+, Triton X-100, Tween 40, and SDS exerted a negative effect on its activity, whereas Mn2+ and 2-mercaptoethanol were found to potentially enhance the activity. Among various kinds of polysaccharide, Paenibacillus sp. TKU052 chitinase exhibited the best catalytic activity on colloidal chitin (CC) with Km = 9.75 mg/mL and Vmax = 2.43 μmol/min. The assessment of the hydrolysis of CC and N-acetyl chitooligosaccharides revealed that Paenibacillus sp. TKU052 chitinase possesses multiple catalytic functions, including exochitinase, endochitinase, and N-acetyl-β-D-glucosaminidase activities. Finally, the combination of Paenibacillus sp. TKU052 chitinase and Streptomyces speibonae TKU048 N-acetyl-β-D-glucosaminidase could efficiently convert CC to N-acetyl-D-glucosamine (GlcNAc) with a production yield of 94.35–98.60% in 12–24 h.

Lysosomal Triglyceride Lipase from the Lateral Line Tissue of Rainbow Trout (Salmo gairdneri)

1971 ◽  
Vol 28 (7) ◽  
pp. 1015-1018 ◽  
Author(s):  
E. Bilinski ◽  
R. E. E. Jonas ◽  
Y. C. Lau
Keyword(s):  
Rainbow Trout ◽  
Lateral Line ◽  
Lysosomal Enzymes ◽  
Lipolytic Activity ◽  
Mitochondrial Fraction ◽  
Maximum Activity ◽  
Salmo Gairdneri ◽  
Acid Lipase ◽  
Triton X ◽  
Hydrolysis Of

An acid lipase active toward tripalmitin and having the characteristics of lysosomal enzymes was shown to occur in the red lateral line tissue of rainbow trout (Salmo gairdneri). The enzyme showed maximum activity at pH 4–4.5. Triton X-100 (0.2–2.0%) strongly stimulated the activity of the acid lipase, but it inhibited markedly the lipolytic activity above pH 7. NaF (20 mM) and Na-p-chloromercuriphenyl-sulfonate (1 mM) partially inhibited the acid lipase. Fractionation of the total homogenate by differential centrifugation in 0.25 M sucrose showed that the acid lipase was present at highest concentration in the light mitochondrial fraction. Palmitic acid and dipalmitin were the two main products of hydrolysis of tripalmitin.

scholarly journals A novel recyclable furoic acid-assisted pretreatment for sugarcane bagasse biorefinery in co-production of xylooligosaccharides and glucose

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Lin Dai ◽  
Tian Huang ◽  
Kankan Jiang ◽  
Xin Zhou ◽  
Yong Xu
Keyword(s):  
Enzymatic Hydrolysis ◽  
Sugarcane Bagasse ◽  
Production Cost ◽  
Solid Loading ◽  
Fed Batch ◽  
Acid Pretreatment ◽  
Furoic Acid ◽  
Cooling Crystallization ◽  
Mineral Acids ◽  
Hydrolysis Of

Abstract Background Pretreatment is the key step for utilizing lignocellulosic biomass, which can extract cellulose from lignin and disrupt its recalcitrant crystalline structure to allow much more effective enzymatic hydrolysis; and organic acids pretreatment with dual benefic for generating xylooligosaccharides and boosting enzymatic hydrolysis has been widely used in adding values to lignocellulose materials. In this work, furoic acid, a novel recyclable organic acid as catalyst, was employed to pretreat sugarcane bagasse to recover the xylooligosaccharides fraction from hemicellulose and boost the subsequent cellulose saccharification. Results The FA-assisted hydrolysis of sugarcane bagasse using 3% furoic acid at 170 °C for 15 min resulted in the highest xylooligosaccharides yield of 45.6%; subsequently, 83.1 g/L of glucose was harvested by a fed-batch operation with a solid loading of 15%. Overall, a total of 120 g of xylooligosaccharides and 335 g glucose could be collected from 1000 g sugarcane bagasse starting from the furoic acid pretreatment. Furthermore, furoic acid can be easily recovered by cooling crystallization. Conclusion This work put forward a novel furoic acid pretreatment method to convert sugarcane bagasse into xylooligosaccharides and glucose, which provides a strategy that the sugar and nutraceutical industries can be used to reduce the production cost. The developed process showed that the yields of xylooligosaccharides and byproducts were controllable by shortening the reaction time; meanwhile, the recyclability of furoic acid also can potentially reduce the pretreatment cost and potentially replace the traditional mineral acids pretreatment.

scholarly journals The roles of phospholipase D and a GTP-binding protein in guanosine 5′-[γ-thio]triphosphate-stimulated hydrolysis of phosphatidylcholine in rat liver plasma membranes

1990 ◽  
Vol 272 (3) ◽  
pp. 749-753 ◽  
Author(s):  
K M Hurst ◽  
B P Hughes ◽  
G J Barritt
Keyword(s):  
Rat Liver ◽  
Phospholipase D ◽  
Plasma Membranes ◽  
Regulatory Protein ◽  
Gtp Binding ◽  
Liver Plasma Membranes ◽  
Low Concentrations ◽  
Rat Liver Plasma Membranes ◽  
Triton X ◽  
Hydrolysis Of

1. Guanosine 5′-[gamma-thio]triphosphate (GTP[S]) stimulated by 50% the rate of release of [3H]choline and [3H]phosphorylcholine in rat liver plasma membranes labelled with [3H]choline. About 70% of the radioactivity released in the presence of GTP[S] was [3H]choline and 30% was [3H]phosphorylcholine. 2. The hydrolysis of phosphorylcholine to choline and the conversion of choline to phosphorylcholine did not contribute to the formation of [3H]choline and [3H]phosphorylcholine respectively. 3. The release of [3H]choline from membranes was inhibited by low concentrations of SDS or Triton X-100. Considerably higher concentrations of the detergents were required to inhibit the release of [3H]phosphorylcholine. 4. Guanosine 5′-[beta gamma-imido]triphosphate and guanosine 5′-[alpha beta-methylene]triphosphate, but not adenosine 5′-[gamma-thio]-triphosphate, stimulated [3H]choline release to the same extent as did GTP[S]. The GTP[S]-stimulated [3H]choline release was inhibited by guanosine 5′-[beta-thio]diphosphate, GDP and GTP but not by GMP. 5. It is concluded that, in rat liver plasma membranes, (a) GTP[S]-stimulated hydrolysis of phosphatidylcholine is catalysed predominantly by phospholipase D with some contribution from phospholipase C, and (b) the stimulation of phosphatidylcholine hydrolysis by GTP[s] occurs via a GTP-binding regulatory protein.

scholarly journals The role of exochitinase type A1 in the fungistatic activity of the rhizosphere bacterium Paenibacillus sp. M4

2016 ◽  
Vol 68 (2) ◽  
pp. 451-459
Author(s):  
Urszula Jankiewicz ◽  
Maria Swiontek-Brzezinska
Keyword(s):  
Plant Pathogens ◽  
Chitinase Activity ◽  
Maximum Activity ◽  
Synergistic Action ◽  
Chitinolytic Activity ◽  
Fungistatic Activity ◽  
Rhizosphere Bacterium ◽  
Paenibacillus Sp ◽  
Growth Inhibiting

The aim of the study was to detect the activity and characterize potentially fungistatic chitinases synthesized by rhizosphere bacteria identified as Paenibacillus sp. M4. Maximum chitinolytic activity was achieved on the fifth day of culturing bacteria in a growth medium with 1% colloidal chitin. Analysis of a zymogram uncovered the presence of four activity bands in the crude bacterial extract. The used three-stage protein purification procedure resulted in a single band of chitinase activity on the zymogram. The purified enzyme exhibited maximum activity at pH 6.5 and temperature 45oC, and thermal stability at 40oC for 4 h. In terms of substrate specificity, it is an exochitinase (chitobiose). The amino acid sequence obtained after mass spectrometry showed similarity to chitinase A1 synthesized by Bacillus circulans. The M4 isolate demonstrated the highest growth inhibiting activity against plant pathogens belonging to the genera Fusarium, Rhizoctonia and Alternaria. Fungistatic activity, although to a somewhat lesser degree, was also demonstrated by purified chitinase. The obtained results confirm the participation of the studied exochitinase in antagonism towards pathogenic molds. However, the lower fungistatic effectiveness of the chitinases points to the synergistic action of different metabolites in biocontrol by these bacteria.

scholarly journals Fungal cellulases: production by solid-state cultivation in packed-bed bioreactor using solid agro-industrial by-products as substrates and application for hydrolysis of sugarcane bagasse

2020 ◽  
pp. 2097-2116 ◽  
Author(s):  
Priscila Aparecida Casciatori Frassatto ◽  
Fernanda Perpétua Casciatori ◽  
João Cláudio Thoméo ◽  
Eleni Gomes ◽  
Maurício Boscolo ◽  
...  
Keyword(s):  
Solid State ◽  
Sugarcane Bagasse ◽  
Enzyme Production ◽  
Packed Bed ◽  
Aeration Rate ◽  
Hydrolysis Time ◽  
Enzymatic Extract ◽  
Packed Bed Bioreactor ◽  
High Concentrations ◽  
Hydrolysis Of

Cellulases are essential for the hydrolysis of lignocellulosic materials in the production of second generation ethanol. Solid-state cultivation is a process that provides high concentrations of enzymes that can be used in this hydrolysis. The objectives of this work were to produce cellulases by cultivating the fungus Myceliophthora thermophila I-1D3b in a packed bed bioreactor with sugarcane bagasse (SCB) and wheat bran (WB) as substrate and to evaluate the efficiency of the enzymatic extract in the hydrolysis of SCB in natura (BIN) and pretreated with ozone, alkali and ultrasound (BOU). The conditions for enzyme production in the bioreactor were SCB:WB at a ratio of 2.3:1 (w/w), 75 % moisture content; 45 ºC; aeration rate 240 L h-1 and 96 h. The enzyme production was evaluated by endoglucanase, xylanase, filter paper (FPU) and ?-glycosidase activities. For the application of the enzymes, a central composed response surface design with 5 repetitions of the central point was used, taking enzyme volume and hydrolysis time as factors. Such cultivation yielded the following enzymatic activities: 723 U gss-1 of endoglucanases, 2024 U gss-1 of xylanase, 12.6 U gss-1 of FPU and 41 U gss-1 of ?-glucosidase. The results of the application tests indicated the best conditions as 7.0 ml of the enzyme extract (4.2 FPU) and 6 hours for BIN and BOU. The best cellulose-glucose conversions were obtained for BOU, reaching 32.1 % at 65 ºC. In conclusion, the enzyme production in the packed bed bioreactor was efficient and BOU pretreatment improved the hydrolysis of biomass, increasing the efficiency of conversion of cellulose to glucose.

scholarly journals A novel recyclable furoic acid-assisted pretreatment for sugarcane bagasse biorefinery in co-production of xylooligosaccharides and glucose

2020 ◽  
Author(s):  
Lin Dai ◽  
Tian Huang ◽  
Kankan Jiang ◽  
Xin Zhou ◽  
Yong Xu
Keyword(s):  
Enzymatic Hydrolysis ◽  
Sugarcane Bagasse ◽  
Production Cost ◽  
Solid Loading ◽  
Fed Batch ◽  
Acid Pretreatment ◽  
Furoic Acid ◽  
Cooling Crystallization ◽  
Mineral Acids ◽  
Hydrolysis Of

Abstract Background: Pretreatment is the key step for utilizing lignocellulosic biomass, which can extract cellulose from lignin and disrupt its recalcitrant crystalline structure to allow much more effective enzymatic hydrolysis; and organic acids pretreatment with dual benefic for generating xylooligosaccharides and boosting enzymatic hydrolysis has been widely used in adding values to lignocellulose materials. In this work, furoic acid, a novel recyclable organic acid as catalyst, was employed to pretreat sugarcane bagasse to recover the xylooligosaccharides fraction from hemicellulose and boost the subsequent cellulose saccharification. Results: The FA-assisted hydrolysis of sugarcane bagasse using 3% furoic acid at 170 oC for 15 min resulted in the highest xylooligosaccharides yield of 45.6%; subsequently, 83.1 g/L of glucose was harvested by a fed-batch operation with a solid loading of 15%. Overall, a total of 120 g of xylooligosaccharides and 335 g glucose could be collected from 1000 g sugarcane bagasse starting from the furoic acid pretreatment. Furthermore, furoic acid can be easily recovered by cooling crystallization.Conclusion: This work put forward a novel furoic acid pretreatment method to convert sugarcane bagasse into xylooligosaccharides and glucose, which provides a strategy that the sugar and nutraceutical industries can be used to reduce the production cost. The developed process showed that the yields of xylooligosaccharides and byproducts were controllable by shortening the reaction time; meanwhile, the recyclability of furoic acid also can potentially reduce the pretreatment cost and potentially replace the traditional mineral acids pretreatment.

scholarly journals Structural and Catalytic Characterization of TsBGL, a β-Glucosidase From Thermofilum sp. ex4484_79

2021 ◽  
Vol 12 ◽  
Author(s):  
Anke Chen ◽  
Dan Wang ◽  
Rui Ji ◽  
Jixi Li ◽  
Shaohua Gu ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Specific Activity ◽  
Maximum Activity ◽  
Homologous Proteins ◽  
Glycosidic Bonds ◽  
Catalytic Sites ◽  
Potential Applications ◽  
Beta Glucosidase ◽  
Hydrolysis Of

Beta-glucosidase is an enzyme that catalyzes the hydrolysis of the glycosidic bonds of cellobiose, resulting in the production of glucose, which is an important step for the effective utilization of cellulose. In the present study, a thermostable β-glucosidase was isolated and purified from the Thermoprotei Thermofilum sp. ex4484_79 and subjected to enzymatic and structural characterization. The purified β-glucosidase (TsBGL) exhibited maximum activity at 90°C and pH 5.0 and displayed maximum specific activity of 139.2μmol/min/mgzne against p-nitrophenyl β-D-glucopyranoside (pNPGlc) and 24.3μmol/min/mgzen against cellobiose. Furthermore, TsBGL exhibited a relatively high thermostability, retaining 84 and 47% of its activity after incubation at 85°C for 1.5h and 90°C for 1.5h, respectively. The crystal structure of TsBGL was resolved at a resolution of 2.14Å, which revealed a classical (α/β)8-barrel catalytic domain. A structural comparison of TsBGL with other homologous proteins revealed that its catalytic sites included Glu210 and Glu414. We provide the molecular structure of TsBGL and the possibility of improving its characteristics for potential applications in industries.

scholarly journals Bioprocessing of Squid Pens Waste into Chitosanase by Paenibacillus sp. TKU047 and Its Application in Low-Molecular Weight Chitosan Oligosaccharides Production

Polymers ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 1163 ◽  
Author(s):  
Chien Thang Doan ◽  
Thi Ngoc Tran ◽  
Van Bon Nguyen ◽  
Trung Dung Tran ◽  
Anh Dzung Nguyen ◽  
...  
Keyword(s):  
Biological Activities ◽  
Radical Scavenging Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Radical Scavenging ◽  
Maximum Activity ◽  
Degree Of Polymerization ◽  
Chitosan Oligosaccharide ◽  
Scavenging Activity ◽  
Paenibacillus Sp

Chitosan oligosaccharide (COS) has become of great interest in recent years because of its worthy biological activities. This study aims to produce COS using the enzymatic method, and investigates Paenibacillus sp. TKU047, a chitinolytic-producing strain, in terms of its chitosanase productivity on several chitinous material-containing mediums from fishery process wastes. The highest amount of chitosanase was produced on the medium using 2% (w/v) squid pens powder (0.60 U/mL) as the single carbon and nitrogen (C/N) source. The molecular mass of TKU047 chitosanase, which could be the smallest one among chitinases/chitosanases from the Paenibacillus genus, was approximately 23 kDa according to the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) method. TKU047 chitosanase possessed the highest activity at 60 °C, pH 7, and toward chitosan solution with a higher degree of deacetylation (DDA) value. Additionally, the hydrolysis products of 98% DDA chitosan catalyzed by TKU047 chitosanase showed the degree of polymerization (DP) ranging from 2 to 9, suggesting that it was an endo-type activity chitosanase. The free radical scavenging activity of the obtained chitosan oligosaccharide (COS) was determined. The result showed that COS produced with Paenibacillus sp. TKU047 chitosanase expressed a higher 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity than that from the commercial COSs with maximum activity and IC50 values of 81.20% and 1.02 mg/mL; 18.63% and 15.37 mg/mL; and 15.96% and 15.16 mg/mL, respectively. As such, Paenibacillus sp. TKU047 may have potential use in converting squid pens waste to produce chitosanase as an enzyme for bio-activity COS preparation.

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