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Cold-active Microfungi and Their Industrial Applications
Published in Ajar Nath Yadav, Ali Asghar Rastegari, Neelam Yadav, Microbiomes of Extreme Environments, 2021
Antifreeze proteins are proteins that can lower the freezing point, by the adsorption-prevention method. They have been reported from bacteria, fungi, polar fishes, insects and plants with their structure being different but action broadly similar. So far five types of fish AFPs and two types of insect AFPs have been described, showing their protein structure and amino acids-composition significantly different from each other (Voets 2017). AFPs are believed to bind to a growing ice surface, shape it to a specific morphology and prevent its further enlargement to assume fatal sizes. AFPs also prevent ice crystals to fuse to form large aggregates (recrystallization) injurious to tissues. AFPs reduce freezing point without affecting melting point (Thermal hysteresis or TH). AFPs from plants exhibit mild TH (0.1–0.5°C), those from fishes moderate TH (1–5°C) and from insects show higher TH (5°C). AFPs from fishes are also found to protect membrane from cold-induced injury. These unique properties of AFPs enable them to act as green or biocryoprotectant for the foods or other biological samples preserved at very low or chilling temperatures.
Large–Scale Freezing and Thawing of Biopharmaceutical Products
Published in Kenneth E. Avis, Vincent L. Wu, Biotechnology and Biopharmaceutical Manufacturing, Processing, and Preservation, 2020
Richard Wisniewski, Vincent Wu
Ice-protein interactions are well researched in the area of protein antifreeze activity. DeVries (1984) and Avanov (1990) support an opinion that antifreeze glycoproteins may form hydrogen bonds with ice crystals and compete with water molecules. Hydroxyl groups of antifreeze molecules play an important role in such hydrogen bond formation. Wen and Laursen (1992) proposed a model for binding antifreeze polypeptides to ice. Hew and Yang (1992) published a review on protein interaction with ice. Proteins can have both inhibiting and promoting influences upon the growth of ice crystals. Results were cited showing the exclusion of sodium chloride ions from ice crystals and the incorporation of antifreeze proteins into the ice structure. The antifreeze proteins adsorb with a preference to certain planes of ice crystals. Since they do not adsorb uniformly to all ice surfaces, they have a detrimental effect upon ice crystal growth. A result of such an effect is a lowering of the temperature of crystal formation (supercooling). It was suggested that ice nucleationpromoting proteins may have a highly repetitive structure and they may consist mostly of beta sheets. The tertiary structure of such ice nucleation proteins may also possess a surface structure that is lattice-matching with ice.
Applications
Published in Raj P. Chhabra, CRC Handbook of Thermal Engineering Second Edition, 2017
Joshua D. Ramsey, Ken Bell, Ramesh K. Shah, Bengt Sundén, Zan Wu, Clement Kleinstreuer, Zelin Xu, D. Ian Wilson, Graham T. Polley, John A. Pearce, Kenneth R. Diller, Jonathan W. Valvano, David W. Yarbrough, Moncef Krarti, John Zhai, Jan Kośny, Christian K. Bach, Ian H. Bell, Craig R. Bradshaw, Eckhard A. Groll, Abhinav Krishna, Orkan Kurtulus, Margaret M. Mathison, Bryce Shaffer, Bin Yang, Xinye Zhang, Davide Ziviani, Robert F. Boehm, Anthony F. Mills, Santanu Bandyopadhyay, Shankar Narasimhan, Donald L. Fenton, Raj M. Manglik, Sameer Khandekar, Mario F. Trujillo, Rolf D. Reitz, Milind A. Jog, Prabhat Kumar, K.P. Sandeep, Sanjiv Sinha, Krishna Valavala, Jun Ma, Pradeep Lall, Harold R. Jacobs, Mangesh Chaudhari, Amit Agrawal, Robert J. Moffat, Tadhg O’Donovan, Jungho Kim, S.A. Sherif, Alan T. McDonald, Arturo Pacheco-Vega, Gerardo Diaz, Mihir Sen, K.T. Yang, Martine Rueff, Evelyne Mauret, Pawel Wawrzyniak, Ireneusz Zbicinski, Mariia Sobulska, P.S. Ghoshdastidar, Naveen Tiwari, Rajappa Tadepalli, Raj Ganesh S. Pala, Desh Bandhu Singh, G. N. Tiwari
A new approach to improving the efficacy of cryosurgery is derived from techniques long applied to enhance cryopreservation processes. Namely, the tissue is modified by addition of chemical agent prior to the initiation of freezing. However, for applications in cryosurgery the desired result is an increased level of cell killing. Antifreeze proteins (AFPs) are proving to be effective for this purpose.235,236 AFPs are chemical compounds synthesized by many differing types of plants and animals to provide protection against freezing injury at high subzero temperatures.237,238 It has also been demonstrated that AFPs modify ice crystals to needlelike shapes that can destroy cells during freezing to deeper subzero temperatures.239
Glutaminase-free L-asparaginase production by Leucosporidium muscorum isolated from Antarctic marine-sediment
Published in Preparative Biochemistry & Biotechnology, 2021
Rominne Karla Barros Freire, Carlos Miguel Nóbrega Mendonça, Rafael Bertelli Ferraro, Ignacio Sánchez Moguel, Aldo Tonso, Felipe Rebello Lourenço, João Henrique Picado Madalena Santos, Lara Durães Sette, Adalberto Pessoa Junior
Previously included in the genus Candida and following in the genera Rhodotorulla and Leucosporidiella,[43] the species Leucosporidiella muscorum was most recently reclassified as Leucosporidium muscorum.[44] Species of Leucosporidiales are known for being isolated predominantly from cold environments and are reported as psychrotolerant yeasts, because they can grow between 4 and 22 °C but not at 30 °C. Moreover, some species are recognized as potential sources of extracellular cold-enzymes and antifreeze proteins.[44]
Extremozymes used in textile industry
Published in The Journal of The Textile Institute, 2022
Priyanka Kakkar, Neeraj Wadhwa
They have adapted unique mechanisms and molecular means to make their cellular components stable from extreme conditions like high pH, temperature, salinity, pressure. For example, to cope with saline environment they increase the amount of compatible solutes in the cell and maintain the osmotic equilibrium by regulating ion pumps. The major changes occurs in the amino acid sequence which further translates to form adaptive structural changes like flexibility, charge, hydrophobicity. Halophiles increase the acid amino acids as their carboxylic side chain competes with cations and in turn stops the aggregation and hydration of the protein. (Brininger et al., 2018; Sarmiento et al., 2015). Psychrophiles have combination of adaptive features to increase protein flexibility like high surface hydrophobicity, less core hydrophobicity, increase in the no. of loops with more glycine and less proline residues, weaker metal binding site, less electrostatic interaction (Cavicchioli et al., 2011). Psychrophiles have less proline residue to increase the flexibility of the protein. For instance psychrophilic α- amylase has 13 proline residues while mesophiles and thermophiles have 19 and 25 proline residues respectively. Proline restricts the rotation of protein backbone by forming nitrogen-pyrrolidine ring structure which locks the dihedral angle of protein. Fewer proline in the structure eventually result in reduced nitrogen-pyrrolidine ring structure and the flexibility of the protein will increase (Brininger et al., 2018). Proteins around catalytic sites also show adaptations to increase mobility of active site, size and number of the protein cavity also increases by packing effect which allows water to enter in the cavities leading to high enzyme flexibility (Paredes et al., 2011) . Besides protein structure adaptation, they also show modification in cell membrane and cell wall structure, membrane pigmentation, production of compatible solutes, chaperones, ice-nucleating proteins, antifreeze proteins (Collins & Margesin, 2019). For example, Pseudomonas putida GR12-2 secretes an antifreeze protein encoded by gene afpA, which makes their survival easier in low temperature. Antifreeze proteins get adsorbed at the ice surface and reduces its temperature and also stops recrystallization (Muryoi et al., 2004). In thermophiles, small but specific modifications are responsible for thermal stability. Adaptations are done by reducing the flexibility of the proteins by forming large hydrophobic core; more hydrophobic residues; decreased loop length. High ionic interactions and increase in the number of disulphide bond prevents the protein from denaturing (Feller, 2018). Amino acid composition like increase in charge (Glu, Arg), non-polar (hydrophobic), aromatic (Tyr) amino acids and decrease in uncharged, thermoliable amino acids contributes to the increase in intrinsic thermal stability of protein (Zhou et al., 2008). All the extremophiles show certain adaptation strategy for survival adaptation as shown in Table 1.