Oxidative cleavage and hydrolytic boosting of cellulose in soybean spent flakes by Trichoderma reesei Cel61A lytic polysaccharide monooxygenase

2017 ◽  
Vol 98 ◽  
pp. 58-66 ◽  
Author(s):  
Brian C. Pierce ◽  
Jane Wittrup Agger ◽  
Jesper Wichmann ◽  
Anne S. Meyer
Keyword(s):  
Trichoderma Reesei ◽  
Oxidative Cleavage ◽  
Lytic Polysaccharide Monooxygenase ◽  
Polysaccharide Monooxygenase

scholarly journals NEW ASPECTS OF THE ENZYMATIC BREAKDOWN OF CHITIN: A REVIEW

2021 ◽  
Vol 26 ◽  
pp. 5-10
Author(s):  
Urszula Jankiewicz ◽  
◽  
Arletta Kochańska-Jeziorska ◽  
Agnieszka Gałązka
Keyword(s):  
Crystalline Structure ◽  
Enzymatic Degradation ◽  
Soluble Sugars ◽  
Practical Importance ◽  
Oxidative Cleavage ◽  
Lytic Polysaccharide Monooxygenase ◽  
Great Practical Importance ◽  
Polysaccharide Monooxygenase

This review focuses on the enzymatic breakdown of chitin, taking into account the latest scientific reports on the activity of lytic polysaccharide monooxygenase (LPMO). Chitin is a natural, abundant polysaccharide of great practical importance in the environment. However, the insolubility in water and the tightly packed crystalline structure of chitin pose a serious obstacle to enzymatic degradation. This substrate can be converted into soluble sugars by the action of glycosidic hydrolases (GH), also known as chitinases. LPMO could prove to be helpful in enzymatic processes that increase the rate of chitin depolymerisation by improving the availability of substrates for chitinases. The unique action of LPMO is based on the ability to catalyse the oxidative cleavage of glycosidic chains present in complex, resistant crystal networks of chitin, and this cleavage facilitates the subsequent action of glycolytic hydrolases.

scholarly journals Comparative Secretomics Analysis Reveals the Major Components of Penicillium oxalicum 16 and Trichoderma reesei RUT-C30

2021 ◽  
Vol 9 (10) ◽  
pp. 2042
Author(s):  
Kexin Wang ◽  
Nian Zhang ◽  
Robin Pearce ◽  
Shi Yi ◽  
Xihua Zhao
Keyword(s):  
Solid State ◽  
Trichoderma Reesei ◽  
Soluble Starch ◽  
Penicillium Oxalicum ◽  
Glycoside Hydrolases ◽  
Lytic Polysaccharide Monooxygenase ◽  
Average Abundance ◽  
Trichoderma Reesei Rut C30 ◽  
Rut C30 ◽  
Polysaccharide Monooxygenase

In this study, the major secretome components of Penicillium oxalicum 16 and Trichoderma reesei RUT-C30 under wheat bran (WB) and rice straw (RS) solid-state fermentation were systematically analyzed. The activities of the major components, e.g., cellulase, hemicellulase, and amylase, were consistent with their abundance in the secretomes. P. oxalicum 16 secreted more abundant glycoside hydrolases than T. reesei RUT-C30. The main up-regulated proteins from the induction of WB, compared with that from RS, were amylase, pectinase, and protease, whereas the main down-regulated enzymes were cellulase, hemicellulase, swollenin, and lytic polysaccharide monooxygenase (LPMO). Specifically, WB induced more β-1,4-glucosidases, namely, S8B0F3 (UniProt ID), and A0A024RWA5 than RS, but RS induced more β-1,4-exoglucanases and β-1,4-endoglucanases, namely, A0A024RXP8, A024SH76, S7B6D6, S7ZP52, A024SH20, A024S2H5, S8BGM3, S7ZX22, and S8AIJ2. The P. oxalicum 16 xylanases S8AH74 and S7ZA57 were the major components responsible for degrading soluble xylan, and S8BDN2 probably acted on solid-state hemicellulose instead of soluble xylan. The main hemicellulase component of T. reesei RUT-C30 in RS was the xyloglucanase A0A024S9Z6 with an abundance of 16%, but T. reesei RUT-C30 lacked the hemicellulase mannanase and had a small amount of the hemicellulase xylanase. P. oxalicum 16 produced more amylase than T. reesei RUT-C30, and the results suggest amylase S7Z6T2 may degrade soluble starch. The percentage of the glucoamylase S8B6D7 did not significantly change, and reached an average abundance of 5.5%. The major auxiliary degradation enzymes of P. oxalicum 16 were LPMOs S7Z716 and S7ZPW1, whereas those of T. reesei RUT-C30 were swollenin and LPMOs A0A024SM10, A0A024SFJ2, and A0A024RZP7.

scholarly journals Correction to “Oxidative Cleavage of Cellobiose by Lytic Polysaccharide Monooxygenase (LPMO)-Inspired Copper Complexes”

ACS Omega ◽  
2020 ◽  
Vol 5 (43) ◽  
pp. 28403-28403
Author(s):  
Andrea. C. Neira ◽  
Paulina R. Martínez-Alanis ◽  
Gabriel Aullón ◽  
Marcos Flores-Alamo ◽  
Paulino Zerón ◽  
...  
Keyword(s):  
Copper Complexes ◽  
Oxidative Cleavage ◽  
Lytic Polysaccharide Monooxygenase ◽  
Polysaccharide Monooxygenase

scholarly journals Oxidative Cleavage of Cellobiose by Lytic Polysaccharide Monooxygenase (LPMO)-Inspired Copper Complexes

ACS Omega ◽  
2019 ◽  
Vol 4 (6) ◽  
pp. 10729-10740 ◽  
Author(s):  
Andrea. C. Neira ◽  
Paulina R. Martínez-Alanis ◽  
Gabriel Aullón ◽  
Marcos Flores-Alamo ◽  
Paulino Zerón ◽  
...  
Keyword(s):  
Copper Complexes ◽  
Oxidative Cleavage ◽  
Lytic Polysaccharide Monooxygenase ◽  
Polysaccharide Monooxygenase

Oxidative cleavage of some cellulosic substrates by auxiliary activity (AA) family 9 enzymes influences the adsorption/desorption of hydrolytic cellulase enzymes

2016 ◽  
Vol 18 (23) ◽  
pp. 6329-6336 ◽  
Author(s):  
Jinguang Hu ◽  
Amadeus Pribowo ◽  
Jack N. Saddler
Keyword(s):  
Oxidative Cleavage ◽  
Lytic Polysaccharide Monooxygenase ◽  
Cellulase Enzymes ◽  
Adsorption Desorption ◽  
Hydrolysis Of ◽  
Polysaccharide Monooxygenase

The addition of Lytic polysaccharide monooxygenase (LPMO's) increases the desorption of exoglucanases during the hydrolysis of cellulosic substrates.

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