scholarly journals Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes

2016 ◽  
Vol 7 ◽  
Author(s):  
Margarita Santiago ◽  
César A. Ramírez-Sarmiento ◽  
Ricardo A. Zamora ◽  
Loreto P. Parra
Keyword(s):  
Molecular Mechanisms ◽  
Industrial Applications ◽  
Cold Active Enzymes ◽  
Cold Active

scholarly journals Taking Advantage of Promiscuity of Cold-Active Enzymes

2020 ◽  
Vol 10 (22) ◽  
pp. 8128
Author(s):  
Sondavid K. Nandanwar ◽  
Shweta Bharat Borkar ◽  
Jun Hyuck Lee ◽  
Hak Jun Kim
Keyword(s):  
Energy Cost ◽  
Active Sites ◽  
Catalytic Efficiency ◽  
Industrial Applications ◽  
Side Reactions ◽  
Structural Flexibility ◽  
Enzymatic Modification ◽  
Cold Active Enzymes ◽  
Cold Active ◽  
Substrate Promiscuity

Cold-active enzymes increase their catalytic efficiency at low-temperature, introducing structural flexibility at or near the active sites. Inevitably, this feat seems to be accompanied by lower thermal stability. These characteristics have made cold-active enzymes into attractive targets for the industrial applications, since they could reduce the energy cost in the reaction, attenuate side-reactions, and simply be inactivated. In addition, the increased structural flexibility could result in broad substrate specificity for various non-native substrates, which is called substrate promiscuity. In this perspective, we deal with a less addressed aspect of cold-active enzymes, substrate promiscuity, which has enormous potential for semi-synthesis or enzymatic modification of fine chemicals and drugs. Further structural and directed-evolutional studies on substrate promiscuity of cold-active enzymes will provide a new workhorse in white biotechnology.

scholarly journals Transcriptome and proteome analysis suggest enhanced photosynthesis in tetraploid Liriodendron sino-americanum

2021 ◽  
Author(s):  
Tingting Chen ◽  
Yu Sheng ◽  
Zhaodong Hao ◽  
Xiaofei Long ◽  
Fangfang Fu ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Protein Complexes ◽  
Proteome Analysis ◽  
Tree Height ◽  
Photosynthetic Electron Transport ◽  
Industrial Applications ◽  
Chlorophyll Protein Complexes ◽  
Chlorophyll Protein ◽  
Photosynthesis Genes ◽  
Underlying Mechanisms

Abstract Polyploidy generally provides an advantage in phenotypic variation and growth vigor. However, the underlying mechanisms remain poorly understood. The tetraploid L. sino-americanum exhibits altered morphology compared to its diploid counterpart, including larger, thicker and deeper green leaves, bigger stomata, thicker stems and increased tree height. Such characteristics can be useful in ornamental and industrial applications. To elucidate the molecular mechanisms behind this variation, we performed a comparative transcriptome and proteome analysis. Our transcriptome data indicated that some photosynthesis genes and pathways were differentially altered and enriched in tetraploid L. sino-americanum, mainly related to F-type ATPase, the cytochrome b6/f complex, photosynthetic electron transport, the light harvesting chlorophyll protein complexes, photosystem I and II. Most of the differentially expressed proteins we could identify are also involved in photosynthesis. Our physiological results showed that tetraploids have an enhanced photosynthetic capacity, concomitant with great levels of sugar and starch in leaves. This suggests that tetraploid L. sino-americanum might experience comprehensive transcriptome reprogramming of genes related to photosynthesis. This study has especially emphasized molecular changes involved in photosynthesis that accompany polyploidy, and provides a possible explanation for the altered phenotype of polyploidy plants in comparison to their diploid form.

scholarly journals Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation

Marine Drugs ◽  
2021 ◽  
Vol 19 (1) ◽  
pp. 43
Author(s):  
Marco Mangiagalli ◽  
Marina Lotti
Keyword(s):  
Low Temperature ◽  
Molecular Mechanisms ◽  
Building Blocks ◽  
Cold Active ◽  
Cold Adaption ◽  
Glycosyl Donor ◽  
Pharmaceutical Industries ◽  
Biotechnological Processes ◽  
Hydrolysis Of ◽  
Insight Into

β-galactosidases (EC 3.2.1.23) catalyze the hydrolysis of β-galactosidic bonds in oligosaccharides and, under certain conditions, transfer a sugar moiety from a glycosyl donor to an acceptor. Cold-active β-galactosidases are identified in microorganisms endemic to permanently low-temperature environments. While mesophilic β-galactosidases are broadly studied and employed for biotechnological purposes, the cold-active enzymes are still scarcely explored, although they may prove very useful in biotechnological processes at low temperature. This review covers several issues related to cold-active β-galactosidases, including their classification, structure and molecular mechanisms of cold adaptation. Moreover, their applications are discussed, focusing on the production of lactose-free dairy products as well as on the valorization of cheese whey and the synthesis of glycosyl building blocks for the food, cosmetic and pharmaceutical industries.

Enzymatic biodegradation of highly p-xylene contaminated soil using cold-active enzymes: A soil column study

2021 ◽  
pp. 127099
Author(s):  
Saba Miri ◽  
Seyyed Mohammadreza Davoodi ◽  
Thomas Robert ◽  
Satinder Kaur Brar ◽  
Richard Martel ◽  
...  
Keyword(s):  
Contaminated Soil ◽  
Soil Column ◽  
Column Study ◽  
Cold Active Enzymes ◽  
Cold Active

Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications

3 Biotech ◽  
2021 ◽  
Vol 11 (11) ◽  
Author(s):  
Megha Kumari ◽  
Srichandan Padhi ◽  
Swati Sharma ◽  
Loreni Chiring Phukon ◽  
Sudhir P. Singh ◽  
...  
Keyword(s):  
Food Processing ◽  
Biotechnological Potential ◽  
Cold Active Enzymes ◽  
Cold Active

Bacterial diversity and bioprospecting for cold-active enzymes from culturable bacteria associated with sediment from a melt water stream of Midtre Loenbreen glacier, an Arctic glacier

2009 ◽  
Vol 160 (8) ◽  
pp. 538-546 ◽  
Author(s):  
Puram Vishnu Vardhan Reddy ◽  
Singireesu Soma Shiva Nageswara Rao ◽  
Mambatta Shankaranarayanan Pratibha ◽  
Buddhi Sailaja ◽  
Bakka Kavya ◽  
...  
Keyword(s):  
Bacterial Diversity ◽  
Culturable Bacteria ◽  
Water Stream ◽  
Cold Active Enzymes ◽  
Melt Water ◽  
Cold Active ◽  
Arctic Glacier

scholarly journals EXTRACELLULAR COLD ACTIVE ENDOGLUCANASE AND PIGMENT PRODUCING PSYCHROTOLERANT PENICILLIUM PINOPHILUM

2016 ◽  
Vol 8 (10) ◽  
pp. 164 ◽  
Author(s):  
Abhas Kumar Maharana
Keyword(s):  
Sugarcane Bagasse ◽  
Endoglucanase Activity ◽  
Total Enzyme Activity ◽  
Cold Active Enzymes ◽  
Red Color ◽  
Cold Active ◽  
Penicillium Pinophilum ◽  
Groundnut Shell ◽  
Color Pigment ◽  
Total Enzyme

<p><strong>Objective: </strong>The objective of the present study was on <em>Penicillium pinophilum </em>strain F2 from soil samples of Jammu city having the potentiality to produce alkaline cold active endoglucanase and pigment.</p><p><strong>Methods: </strong><em>Penicillium pinophilum </em>strain F2,<em> </em>a<em> </em>psychrotolerant micro-fungus was isolated from soil of Jammu city, India by taking Czapek’s Dox agar incubated at 15 °C. The strain was screened for production of cold active enzymes by taking various substrates at 15 °C. Final production was done for cold active endoglucanase by using sugarcane bagasse and ground nut shell as substrates. Besides, the strain was also able to produce red color pigment at a low temperature which was further studied to optimize its production by changing pH and growth medium. The produced pigment was used for dyeing of wool and silk, and absorption percentages were also calculated.</p><p><strong>Results: </strong>Screening for the production of cold active enzymes revealed it as a good producer of cellulose followed by lipase and amylase. Endoglucanase production revealed the total enzyme titer (total enzyme activity) was found to be 5.032 folds higher in sugarcane bagasse (38.91 units) than groundnut shell (7.732 units). Endoglucanase activity was maximum 9.82±0.33 units/ml and 2.29±0.31 units/ml after 120 h of incubation at 15 °C by sugarcane bagasse and groundnut shells, respectively. Red color pigment production was maxima at pH 5 in Czapek’s Dox broth. Maximum absorption percentage was seen by the treatment soaked with mordant, i.e. 5% CuSO<sub>4 </sub>(51.52%) and without a mordant, it showed about 45.54%.</p><p><strong>Conclusion: </strong>Due to the above unique features and capability to produce cold active endoglucanase and pigment by strain F2, can be used significantly in various industries.</p>

scholarly journals Aliivibrio wodanis as a production host: development of genetic tools for expression of cold-active enzymes

2019 ◽  
Vol 18 (1) ◽  
Author(s):  
Jenny Johansson Söderberg ◽  
Miriam Grgic ◽  
Erik Hjerde ◽  
Peik Haugen
Keyword(s):  
Low Temperature ◽  
Protein Production ◽  
Fluorescent Protein ◽  
Active Form ◽  
Rhodococcus Erythropolis ◽  
Expression Systems ◽  
Cold Adapted ◽  
Genetic Tools ◽  
Cold Active Enzymes ◽  
Cold Active

Abstract Background Heterologous production of cold-adapted proteins currently represents one of the greatest bottlenecks in the ongoing bioprospecting efforts to find new enzymes from low-temperature environments, such as, the polar oceans that represent essentially untapped resources in this respect. In mesophilic expression hosts such as Escherichia coli, cold-adapted enzymes often form inactive aggregates. Therefore it is necessary to develop new low-temperature expression systems, including identification of new host organisms and complementary genetic tools. Psychrophilic bacteria, including Pseudoalteromonas haloplanktis, Shewanella and Rhodococcus erythropolis have all been explored as candidates for such applications. However to date none of these have found widespread use as efficient expression systems, or are commercially available. In the present work we explored the use of the sub-Arctic bacterium Aliivibrio wodanis as a potential host for heterologous expression of cold-active enzymes. Results We tested 12 bacterial strains, as well as available vectors, promoters and reporter systems. We used RNA-sequencing to determine the most highly expressed genes and their intrinsic promoters in A. wodanis. In addition we examined a novel 5′-fusion to stimulate protein production and solubility. Finally we tested production of a set of “difficult-to-produce” enzymes originating from various bacteria and one Archaea. Our results show that cold-adapted enzymes can be produced in soluble and active form, even in cases when protein production failed in E. coli due to the formation of inclusion bodies. Moreover, we identified a 60-bp/20-aa fragment from the 5′-end of the AW0309160_00174 gene that stimulates expression of Green Fluorescent Protein and improves production of cold-active enzymes when used as a 5′-fusion. A 25-aa peptide from the same protein enhanced secretion of a 25-aa-sfGFP fusion. Conclusions Our results indicate the use of A. wodanis and associated genetic tools for low-temperature protein production and indicate that A. wodanis represents an interesting platform for further development of a protein production system that can promote further cold-enzyme discoveries.

Biotechnological Aspects of Cold-Active Enzymes

2017 ◽  
pp. 461-475 ◽  
Author(s):  
Mário Barroca ◽  
Gustavo Santos ◽  
Charles Gerday ◽  
Tony Collins
Keyword(s):  
Cold Active Enzymes ◽  
Cold Active
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