Manno‐oligosaccharide preparation by the hydrolysis of konjac flour with a thermostable endo‐mannanase from Talaromyces cellulolyticus

Abstract

Aims A thermostable endo‐mannanase from the fungus Talaromyces cellulolyticus was identified to facilitate manno‐oligosaccharide preparation from Konjac (Amorphophallus konjac) flour. Methods and Results A putative endo‐1,4‐β‐mannanase from the T. cellulolyticus was obtained and efficiently expressed by improving its gene dosage in the genome of the host. After cultivation in a bench‐top bioreactor for about 120 h, the protein content and enzyme activity of mannanase increased to 3·4 g l−1 and 17 500 U ml−1 respectively. Enzymatic characterization showed that this enzyme has an optimal temperature of 80°C, optimal pH of 5·0. Under the optimized hydrolysis conditions of pH 5·0, 70°C, and an enzyme concentration of 200 U l−1 solution, this enzyme could efficiently hydrolyse 0·5% konjac flour into manno‐oligosaccharides (MOSs) with the degree of polymerization range from 3 to 7. The possible mechanism by which the enzyme produced MOSs was also discussed. Conclusion Talaromyces cellulolyticus endo‐mannanase is thermostable and has a broad pH range adaptability. Method of improving the dosage of mannanase gene in the genome could realized its high‐level impression. This enzyme could efficiently hydrolyse konjac flour into manno‐oligosaccharide products. Significance and Impact of the Study This study has enriched endo‐mannanase resources, facilitated its bulk production and provided a strong reference for its application in manno‐oligosaccharide preparation from the natural glucomannan of konjac flour.

Mannooligosaccharide production by β‐mannanase enzyme application from coffee extract

“…As for the hydrolysis products of locust bean gum, they were reported as M2, M3, and M4 (Ichinose et al, 2017). In the literature, there are numerous studies related to MOS production from mannan and agro-waste mannans (Ariandi, Yopi, & Meryandini, 2015;Jana & Kango, 2020;Jana, Suryawanshi, Prajapati, Soni, & Kango, 2018;Li et al, 2018Li et al, , 2020Liu et al, 2018Liu et al, , 2020Pangsri, Piwpankaew, Ingkakul, Nitisinprasert, & Keawsompong, 2015;Rahmani, Amanah, Santoso, & Lisdiyanti, 2020;Rahmani et al, 2017;Rungruangsaphakun & Keawsompong, 2018;Sachslehner et al, 2000;Suryawanshi, Jana, Prajapati, & Kango, 2019;Tian, Freeman, Corey, German, & Barile, 2017;Yang, Chen, Zhou, Wang, & Liu, 2019;Yilmazer, Germec, & Turhan, 2020;Zang et al, 2015). When examining the existing results in the literature, they assisted the results of the present study and was tremendously compatible with them.…”

Reshaping the binding channel of a novel GH113 family β-mannanase from Paenibacillus cineris (PcMan113) for enhanced activity

“…MOS are generally produced via the enzymatic hydrolysis of LBG, KG, and GG due to the higher extraction efficiency, environmental benefits, lower cost, and easy processing (Yang et al 2019 ). Based on present reports on the preparation of MOS, several enzymes, such as mannanases, mannosidases, galactosidases and glucosidases, must work in synergy to achieve the desired degree of polymerization (Malgas et al 2015 ).…”

“…(Shimizu et al 2015 ) cannot meet the increasing demand for food-grade MOS products. Although a number of studies focused on the identification of new β-mannanases to prepare MOS from one or two kinds of mannans, there are only a few reports on β-mannanases belonging to the GH113 family that can effectively hydrolyze LBG, KG, and GG for the preparation of MOS (Cao et al 2018 ; Yang et al 2019 , 2015 ; Li et al 2017 ). Furthermore, finding mannanases with high activity and stability during the catalytic process is essential for industrial application in MOS production.…”

Reshaping the binding channel of a novel GH113 family β-Mannanase from Paenibacillus cineris (PcMan113) for enhanced activity

“…(Zhang et al 2008 nding mannanases with high activity and stability during the catalytic process is essential for industrial application in MOS production. Therefore, mannanases which have speci c characteristics, such as higher activity, acid resistance and thermal stability, are currently required (Yang et al 2019).…”

“…MOS are generally produced via the enzymatic hydrolysis of LBG, KG, and GG due to the higher extraction e ciency, environmental bene ts, lower cost, and easy operation (Yang et al 2019). Based on present reports on the preparation of MOS, several enzymes, such as mannanases, mannosidases, galactosidases and glucosidases, must work in synergy to achieve the desired degree of polymerization (Malgas et al 2015).…”