Biotechnological Eminence of Chitinases: A Focus on Thermophilic Enzyme Sources, Production Strategies and Prominent Applications.

2021 ◽  
Vol 28 ◽  
Author(s):  
Fatima Akram ◽  
Rabia Akram ◽  
Ikram ul Haq ◽  
Ali Nawaz ◽  
Zuriat Jabbar ◽  
...  
Keyword(s):  
Specific Activity ◽  
High Specific Activity ◽  
Industrial Applications ◽  
Thermostable Enzyme ◽  
Raw Material ◽  
Thermostable Enzymes ◽  
Thermophilic Microorganisms ◽  
Industrial Processing ◽  
Glycosidic Bonds ◽  
Renewable Raw Material

Background: Chitin, the second most abundant polysaccharide in nature, is a constantly valuable and renewable raw material after cellulose. Due to advancement in technology, industrial interest has grown to take advantage of the chitin. Objective: Now, biomass is being treated with diverse microbial enzymes or cells for the production of desired products under best industrial conditions. Glycosidic bonds in chitin structure are degraded by chitinase enzymes, which are characterized into number of glycoside hydrolase (GHs) families. Methods: Thermophilic microorganisms are remarkable sources of industrially important thermostable enzymes, having ability to survive harsh industrial processing conditions. Thermostable chitinases have an edge over mesophilic chitinases as they can hydrolyse the substrate at relatively high temperatures and exhibit decreased viscosity, significantly reduced contamination risk, thermal and chemical stability and increased solubility. Various methods are employed to purify the enzyme and increase its yield by optimizing various parameters such as temperature, pH, agitation, and by investigating the effect of different chemicals and metal ions etc. Results: Thermostable chitinase enzymes show high specific activity at elevated temperature which distinguish them from mesophiles. Genetic engineering can be used for further improvement of natural chitinases, and unlimited potential for the production of thermophilic chitinases has been highlighted due to advancement in synthetic biological techniques. Thermostable chitinases are then used in different fields such as bioremediation, medicine, agriculture and pharmaceuticals. Conclusion: This review will provide information about chitinases, biotechnological potential of thermostable enzyme and the methods by which they are being produced and optimized for several industrial applications. Some of the applications of thermostable chitinases have also been briefly described.

scholarly journals Insecticide’s Disappearance after Field Treatment and during Processing into Byproducts

2021 ◽  
Author(s):  
Alberto Angioni ◽  
Nicola Arru
Keyword(s):  
Degradation Rate ◽  
Dilution Effect ◽  
Life Time ◽  
Industrial Applications ◽  
Raw Material ◽  
Epicuticular Waxes ◽  
Industrial Processing ◽  
Table Olive ◽  
Major Factors ◽  
Processing Techniques

Insecticide\'s disappearance after field treatments could be ascribed to different factors such as sunlight photodegradation, dilution effect due to fruit growth, co-distillation during fruit respiration and evaporation. Moreover, the epicuticular waxes could speed or slow down the degradation rate, and the cultivation in an open field or greenhouses could affect the residues dramatically. After harvest, the processing techniques to produce byproducts deeply influence insecticide residues. For example, fruit drying, winemaking, the industrial processing of tomatoes to produce purée, triple-concentrated paste, fine pulp, diced, olive processing to obtain table olive and olive oil, and other industrial applications on fruits affect residues and their half-life time. The scope of this chapter is to highlight the major factors responsible for the disappearance of insecticides after treatment. Moreover, the chapter intends to review the influence of the industrial processes on insecticide behaviour when the raw material is transformed into its byproducts.

scholarly journals Preliminary X-ray diffraction analysis of a thermophilic β-1,3–1,4-glucanase fromClostridium thermocellum

2014 ◽  
Vol 70 (7) ◽  
pp. 946-948 ◽  
Author(s):  
Lilan Zhang ◽  
Puya Zhao ◽  
Chun-Chi Chen ◽  
Chun-Hsiang Huang ◽  
Tzu-Ping Ko ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Specific Activity ◽  
High Specific Activity ◽  
Diffusion Method ◽  
X Ray Diffraction ◽  
Unit Cell Parameters ◽  
X Ray ◽  
Cell Parameters ◽  
Glycosidic Bonds ◽  
Hydrolysis Of

β-1,3–1,4-Glucanases catalyze the specific hydrolysis of internal β-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked β-glucans. The thermophilic glycoside hydrolase CtGlu16A fromClostridium thermocellumexhibits superior thermal profiles, high specific activity and broad pH adaptability. Here, the catalytic domain of CtGlu16A was expressed inEscherichia coli, purified and crystallized in the trigonal space groupP3121, with unit-cell parametersa=b= 74.5,c= 182.9 Å, by the sitting-drop vapour-diffusion method and diffracted to 1.95 Å resolution. The crystal contains two protein molecules in an asymmetric unit. Further structural determination and refinement are in progress.

scholarly journals ISOLATION OF THERMOPHILIC LIPASE PRODUCING BACTERIUM FROM HOT SPRINGS AT THE EAST COAST OF PENINSULAR MALAYSIA

2021 ◽  
Vol 11 (1) ◽  
pp. 1-10
Author(s):  
Tengku Hamid ◽  
◽  
Nur Abidin ◽  
Nurmusfirah Hasan ◽  
◽  
...  
Keyword(s):  
Hot Springs ◽  
East Coast ◽  
Hot Spring ◽  
Thermophilic Bacteria ◽  
Natural Habitat ◽  
Primary Source ◽  
Industrial Applications ◽  
Peninsular Malaysia ◽  
Thermostable Enzymes ◽  
Thermophilic Microorganisms

Hot spring is a natural habitat for thermophilic bacteria and the primary source of thermostable enzymes useful in industrial applications. In Malaysia, the search for thermophilic organisms has been focused on hot springs, especially on the peninsular West coast. In this work, lipase or esterase producing thermophilic microorganisms were isolated from East coast hot springs in Pahang and Terengganu's states. Morphological and biochemical analysis were carried out on Isolates LH1, LH2, LH3, LH4, LH5, B2B2 and S1B4, which showed that they are gram positive, aerobic, spore forming, and motile organisms. All of the seven isolates showed the ability to grow at 45°C and formed hydrolysis zones on tributyrin agar plates. However, only isolate B2B2 and S1B4 were able to thrive at higher temperatures of up to 65°C. The genotypic characterisation was carried out using 16S rRNA sequencing. Bacillus and Geobacillus species were found to be the dominant bacteria isolated from these hot springs. From La hot spring, isolate LH1 (MT 645486), Isolates LH2 (MT645483), LH3 (MT645484), LH4 (MT 645485) and LH5 (MT 645487) were all closely related to Bacillus sp. (at 97.3-97.9%). Meanwhile, from Bentong and Sungai Lembing hot springs, isolates B2B2 (MT668631) and S1B4 (MT668632) were near related to either Geobacillus kaustophilus or Geobacillus thermoleovorans; each at 98.5% and 97.9% similarity, respectively. These strains from Geobacillus sp. were able to thrive at higher temperature and their thermostable esterases or lipases have properties useful for biotechnological applications.

scholarly journals Thermostable Chitosanase from Bacillus sp. Strain CK4: Cloning and Expression of the Gene and Characterization of the Enzyme

2000 ◽  
Vol 66 (9) ◽  
pp. 3727-3734 ◽  
Author(s):  
Ho-Geun Yoon ◽  
Hee-Yun Kim ◽  
Young-Hee Lim ◽  
Hye-Kyung Kim ◽  
Dong-Hoon Shin ◽  
...  
Keyword(s):  
Gene Sequence ◽  
Specific Activity ◽  
High Specific Activity ◽  
Industrial Applications ◽  
Cloning And Expression ◽  
Rrna Gene ◽  
Phenotypic Analysis ◽  
Reading Frame ◽  
The 16S Rrna Gene

ABSTRACT A thermostable chitosanase gene from the environmental isolateBacillus sp. strain CK4, which was identified on the basis of phylogenetic analysis of the 16S rRNA gene sequence and phenotypic analysis, was cloned, and its complete DNA sequence was determined. The thermostable chitosanase gene was composed of an 822-bp open reading frame which encodes a protein of 242 amino acids and a signal peptide corresponding to a 30-kDa enzyme. The deduced amino acid sequence of the chitosanase from Bacillus sp. strain CK4 exhibits 76.6, 15.3, and 14.2% similarities to those from Bacillus subtilis, Bacillus ehemensis, and Bacillus circulans, respectively. C-terminal homology analysis shows thatBacillus sp. strain CK4 belongs to cluster III withB. subtilis. The gene was similar in size to that of the mesophile B. subtilis but showed a higher preference for codons ending in G or C. The enzyme contains 2 additional cysteine residues at positions 49 and 211. The recombinant chitosanase has been purified to homogeneity by using only two steps with column chromatography. The half-life of the enzyme was 90 min at 80�C, which indicates its usefulness for industrial applications. The enzyme had a useful reactivity and a high specific activity for producing functional oligosaccharides as well, with trimers through hexamers as the major products.

scholarly journals Lignin-Based High-Performance Fibers by Textile Spinning Techniques

Materials ◽  
2021 ◽  
Vol 14 (12) ◽  
pp. 3378
Author(s):  
Yanhong Jin ◽  
Jiaxian Lin ◽  
Yu Cheng ◽  
Chunhong Lu
Keyword(s):  
Molecular Weight ◽  
High Performance ◽  
Mechanical Performance ◽  
Direct Conversion ◽  
Industrial Applications ◽  
Fiber Spinning ◽  
Raw Material ◽  
Spinning Process ◽  
Renewable Raw Material ◽  
Modified Lignin

As a major component of lignocellulosic biomass, lignin is one of the largest natural resources of biopolymers and, thus, an abundant and renewable raw material for products, such as high-performance fibers for industrial applications. Direct conversion of lignin has long been investigated, but the fiber spinning process for lignin is difficult and the obtained fibers exhibit unsatisfactory mechanical performance mainly due to the amorphous chemical structure, low molecular weight of lignin, and broad molecular weight distribution. Therefore, different textile spinning techniques, modifications of lignin, and incorporation of lignin into polymers have been and are being developed to increase lignin’s spinnability and compatibility with existing materials to yield fibers with better mechanical performance. This review presents the latest advances in the textile fabrication techniques, modified lignin-based high-performance fibers, and their potential in the enhancement of the mechanical performance.

scholarly journals Development of a Hybrid Bioinorganic Nanobiocatalyst: Remarkable Impact of the Immobilization Conditions on Activity and Stability of β-galactosidase

Molecules ◽  
2021 ◽  
Vol 26 (14) ◽  
pp. 4152
Author(s):  
Luigi Tavernini ◽  
Oscar Romero ◽  
Carla Aburto ◽  
Fernando López-Gallego ◽  
Andrés Illanes ◽  
...  
Keyword(s):  
High Efficiency ◽  
Specific Activity ◽  
High Specific Activity ◽  
Structural Features ◽  
Industrial Applications ◽  
Ion Binding ◽  
Enzyme Recovery ◽  
Biomineralization Process ◽  
In Silico Study ◽  
Ion Binding Sites

Hybrid bioinorganic biocatalysts have received much attention due to their simple synthesis, high efficiency, and structural features that favor enzyme activity and stability. The present work introduces a biomineralization strategy for the formation of hybrid nanocrystals from β-galactosidase. The effects of the immobilization conditions were studied, identifying the important effect of metal ions and pH on the immobilization yield and the recovered activity. For a deeper understanding of the biomineralization process, an in silico study was carried out to identify the ion binding sites at the different conditions. The selected β-galactosidase nanocrystals showed high specific activity (35,000 IU/g biocatalyst) and remarkable thermal stability with a half-life 11 times higher than the soluble enzyme. The nanobiocatalyst was successfully tested for the synthesis of galacto-oligosaccharides, achieving an outstanding performance, showing no signs of diffusional limitations. Thus, a new, simple, biocompatible and inexpensive nanobiocatalyst was produced with high enzyme recovery (82%), exhibiting high specific activity and high stability, with promising industrial applications.

scholarly journals Rational engineering of low temperature activity in thermoalkalophilic Geobacillus thermocatenulatus lipase

2021 ◽  
Author(s):  
Weigao Wang ◽  
Siva Dasetty ◽  
Sapna Sarupria ◽  
Mark Blenner
Keyword(s):  
Active Sites ◽  
Specific Activity ◽  
Industrial Applications ◽  
Significant Activity ◽  
Wild Type ◽  
Thermostable Enzymes ◽  
Adaptation Mechanism ◽  
Thermophilic Enzymes ◽  
Cold Activity ◽  
Geobacillus Thermocatenulatus

While thermophilic enzymes have thermostability desired for broad industrial applications, they can lose activity at ambient temperatures far from their optimal. Engineering cold activity into thermophilic enzymes has the potential to broaden the range of temperatures resulting in significant activity (i.e., decreasing the temperature dependence of kcat). Even though it has been widely suggested that cold temperature enzyme activity results from active flexibility that is at odds with the rigidity necessary for thermostable enzymes; however, directed evolution experiments have shown us these properties are not mutually exclusive. In this study, rational protein engineering was used to introduce flexibility inducing mutations around the active sites of Geobacillus thermocatenulatus lipase (GTL). Two mutants were found to have enhanced specific activity compared to wild-type at temperatures between 283 K to 363 K with p-nitrophenol butyrate but not with larger substrates. Kinetics assay revealed both mutations resulted in psychrophilic traits, such as lower activation enthalpy and more negative entropy values compared to wild type in all substrates. Furthermore, the mutants had significantly improved thermostability compared to wild type enzyme, which proves that it is feasible to improve the cold activity without trade-off. Our study provides insight into the enzyme cold adaptation mechanism and design principles for engineering cold activity into thermostable enzymes.

Effects of Heparin Oligosaccharides with High Affinity for Antithrombin III in Experimental Venous Thrombosis

1982 ◽  
Vol 47 (03) ◽  
pp. 244-248 ◽  
Author(s):  
D P Thomas ◽  
Rosemary E Merton ◽  
T W Barrowcliffe ◽  
L Thunberg ◽  
U Lindahl
Keyword(s):  
Antithrombin Iii ◽  
Specific Activity ◽  
High Specific Activity ◽  
Factor Xa ◽  
Blood Levels ◽  
Thrombin Time ◽  
High Affinity ◽  
Very High

SummaryThe in vitro and in vivo characteristics of two oligosaccharide heparin fragments have been compared to those of unfractionated mucosal heparin. A decasaccharide fragment had essentially no activity by APTT or calcium thrombin time assays in vitro, but possessed very high specific activity by anti-Factor Xa assays. When injected into rabbits at doses of up to 80 ¼g/kg, this fragment was relatively ineffective in impairing stasis thrombosis despite producing high blood levels by anti-Xa assays. A 16-18 monosaccharide fragment had even higher specific activity (almost 2000 iu/mg) by chromogenic substrate anti-Xa assay, with minimal activity by APTT. When injected in vivo, this fragment gave low blood levels by APTT, very high anti-Xa levels, and was more effective in preventing thrombosis than the decasaccharide fragment. However, in comparison with unfractionated heparin, the 16-18 monosaccharide fragment was only partially effective in preventing thrombosis, despite producing much higher blood levels by anti-Xa assays.It is concluded that the high-affinity binding of a heparin fragment to antithrombin III does not by itself impair venous thrombogenesis, and that the anti-Factor Xa activity of heparin is only a partial expression of its therapeutic potential.

Autoprothrombin C Activity from Prothrombin with Snake Venom or Trypsin

1962 ◽  
Vol 08 (03) ◽  
pp. 425-433 ◽  
Author(s):  
Ewa Marciniak ◽  
Edmond R Cole ◽  
Walter H Seegers
Keyword(s):  
Snake Venom ◽  
Thrombolytic Agent ◽  
Sodium Citrate ◽  
Specific Activity ◽  
High Specific Activity ◽  
Citrate Solution ◽  
Clotting Factors ◽  
Activation Products ◽  
Russell’S Viper ◽  
Autoprothrombin C

SummarySuitable conditions were found for the generation of autoprothrombin C from purified prothrombin with the use of Russell’s viper venom or trypsin. DEAE chromatographed prothrombin is structurally altered and has never been found to yield autoprothrombin C and also did not yield it when Russell’s viper venom or trypsin were used. Autoprothrombin C is derived from prothrombin with tissue extract thromboplastin, but not in large amounts with the intrinsic clotting factors. With the latter thrombin and autoprothrombin III are the chief activation products. Autoprothrombin III concentrates were prepared from serum and upon activation with 25% sodium citrate solution or with Russell’s viper venom large amounts of autoprothrombin C were obtained, and this was of high specific activity. Theoretically trypsin is not a thrombolytic agent, but on the contrary should lead to intravascular clotting.

UNIDO, Industrial Processing of Natural Resources. New York: United Nations. 1981. viii + 78pp.US $ 5.00. [United Nations Publication Sales No. E. 81. 11 . B.1]

1982 ◽  
Vol 21 (4) ◽  
pp. 329-333
Author(s):  
Rashid Aziz
Keyword(s):  
New York ◽  
United Nations ◽  
Industrial Development ◽  
Raw Materials ◽  
Developed Countries ◽  
Raw Material ◽  
Industrial Processing ◽  
Depth Study ◽  
Manufactured Exports ◽  
Year 2000

The book under review is a concise but fairly in-depth study of the prospects for export diversification from the Less Developed Countries (henceforth labeled as LDCs) particularly to Developed Countries (henceforth labeled as OCs). Given the multiple problems faced by the LOCs in exporting to the OCs - protectionist policies with regards to manufactured exports, volatility of prices obtained for raw material exports, etc. - the study analyses the potential for following an intermediate route. The important issues in the export of semi -processed and wholly processed raw materials are discussed. 111ese issues range from the problems and potentials for the location of processing facilities in the LOCs to the formulation of appropriate policies to encourage an export of processed goods rather than raw materials. Such policies will be useful both in solving the balance of-payments problems of the LDCs and in attaining the goal of the Lima Declaration and Plan of Action on Industrial Development and Co-operation, that called for 2S percent of world industrial production to be located in the LOCs by the year 2000.

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