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Biotechnological Intercession in Biofuel Production
Published in Rouf Ahmad Bhat, Moonisa Aslam Dervash, Khalid Rehman Hakeem, Khalid Zaffar Masoodi, Environmental Biotechnology, 2022
Wasia Showkat, Moonisa Aslam Dervash, Khalid Z. Masoodi, Javeed A. Mugloo, S. A. Gangoo, Saba Mir
Under fermentation conditions, “CAD1 and COMT” down-regulated “Brachypodium distachyon” plants produced 9% and 17% more ethyl alcohol than control (Papp et al., 2016). About 46% and 44% enhancement in saccharification efficiencies can be demonstrated by two “B. distachyon” mutants that exhibit point mutations at diverse locations in the “CAD gene.” Lignin reduction in these species proves to be quite fruitful for saccharification competence. Five brown midrib (bm) maize mutants and four bm sorghum mutants possessing decreased lignin, have been characterized as “CAD or COMT mutants” which resulted in 22% and 21% amplification in the alteration of cellulose to ethyl alcohol, respectively, thereby increasing digestibility (Bansal et al., 2018). Saccharification efficiency shows three-fold increase due to overexpression of polygalacturonase or pectin methylesterase in transgenic “Arabidopsis.” tobacco and wheat leaves, with the alteration of pectin composition or architecture (Papanikolaou and Aggelis, 2019). Additionally, transgenic stems also show increased efficiency of enzymatic saccharification. Pectin degradation in poplar by overexpression of pectate lyase (that degrades HG) leads to upgradation in wood saccharification, as a consequence of the higher liberation of pentoses and hexoses (Ghildiyal et al., 2017).
Fondamental Aspects of Secretory Enzyme Production by Recombinant Microbes
Published in Yoshikatsu Murooka, Tadayuki Imanaka, Recombinant Microbes for Industrial and Agricultural Applications, 2020
Noboru Takizawa, Mitsuo Yamashita, Yoshikatsu Murooka
Some homologues of the pullulanase secretion factors have been identified in various gram-negative bacteria in the last few years. The xcpA, xcpY, and xcpZ genes are required for extracellular secretion of protein in Pseudomonas aeruginosa [118]. The products of the genes share highly significant homologies with the PulO, PulL, and PulM proteins, respectively [119,120]. Although pulL, and pulM did not complement the xcpY52 and xcpZ52 mutations of P. aeruginosa, pulO could complement the xcpA mutation [121]. The out genes in Erwinia chrysanthemi are responsible for the efficient extracellular secretion of plant cell wall-degrading enzymes, such as pectate lyase and cellulase. The four genes in the out cluster are homologous to the pulH, puU, and pulK genes [121]. In Xanthomonas campestris pathovar campestris, the six gene products (XpsE, -F, -G, -H, -I, -J) in the cluster encoding protein secretion and pathogenicity also show homologies with the PulE, -F, -G, -H, -I, and -J [122]. The adjacent gene, xpsD, also showed significant homology with pulD [123]. These results suggest that the same extracellular secretion systems as those of pullulanase exist widely in the gram-negative bacteria, and that these mechanisms enable secretion of several secretory proteins in a cell. The pullulanase secretion system may also promote secretion of any other protein that is unidentified in Klebsiella.
Role of carbohydrate active enzymes (CAZymes) in production of marine bioactive oligosaccharides and their pharmacological applications
Published in Antonio Trincone, Enzymatic Technologies for Marine Polysaccharides, 2019
As the CPs are very recalcitrant toward conversion to oligosaccharides, efficient conversion of CPs into oligosaccharides is enhanced by employing multidomain CAZymes rather than using enzymes having single catalytic modules. In multidomain CPs-degrading CAZymes, the catalytic modules are appended with more than one noncatalytic ancillary CBMs that are known to promote enzyme activity. Modular CPs-degrading CAZymes have been identified in the genome of marine bacteria. Several CAZymes from S. degradans have novel combinations of noncatalytic CBMs (Weiner et al. 2008). The β-agarase II (AgaE Sde-2655) of S. degradans are appended with three CBM6 modules (Figure 16.2). Additionally, the endoglucanase 5A of S. degradans have two catalytic GH5 modules and is appended with three CBM6 modules (Figure 16.2). S. degradans also encodes highly modular putative manan endo-1,4-β-mannosidase, putative bifunctional xylanase/α-l-arabinofuranosidase, pectin/pectate lyase, alginate lyase, and bifunctional xylanase/acetylxylan esterase (Figure 16.2). The modular α-agarase and alginate lyase are also reported from Alteromonas agarilytica and Flammeovirga sp. MY04, respectively (Figure 16.2). In addition to S. degradans genome, M. mangrovi is a potential source of CPs-degrading CAZymes appended with CBMs (Imran et al. 2017).
Understanding the effects of process parameters in the bioscouring of cotton and their interactions on pectate lyase activity by factorial design analysis
Published in The Journal of The Textile Institute, 2025
Bruna Lyra Colombi, Quesli Martins, Cintia Kopsch Imme, Diofer Barboza Da Silva, José Alexandre Borges Valle, Jürgen Andreaus, Manuel José Lis Arias, Rita De Cássia Siqueira Curto Valle
Pectate lyase enzyme is widely employed in bioscouring of natural cellulosic fibers, especially cotton, for the degradation of the pectin layer on the fiber to grant hydrophilicity and allowing subsequent dyeing, printing, and finishing processes (Andreaus et al., 2019; Besegatto et al., 2018). Pectate lyase requires Ca2+ for activity, has an optimum pH for the action in the alkaline region (7.5-10.0), and has an optimum temperature between 40 and 50°C (Uenojo & Pastore, 2007). Bioprep® 3000 L enzyme, specifically, acts efficiently in specific conditions of the pH between 7 and 9 and temperature between 50 and 60°C (Foulk et al., 2008). Along with the enzyme, surfactants are used in many bioscouring formulations. Surfactants act as emulsifiers and detergents for immiscible fatty substances from the fiber surface and make saponification of these hydrophobic impurities (oils and waxes) in the aqueous medium, increasing the wettability of fabrics (Raza et al., 2014). However, if the surfactant interacts with the enzyme, conformational changes may eventually lead to the loss of enzymatic activity (Holmberg, 2018).