Department of Microbiology and Biotechnology Centre, Faculty of Science, The Maharaja Sayajirao University of Baroda, Vadodara, Gujarat, India.
J Appl Microbiol. 2018 May;124(5):1147-1163. doi: 10.1111/jam.13718. Epub 2018 Mar 13.
The aim of this study was to evaluate the physicochemical properties of the crude pectinase activity from three Bacillus isolates of ruminant dung origin and study their synergism with crude xylanases from the same Bacillus spp. and a commercial cellulase to evaluate their accessory role in improved biomass saccharification.
Pectinolytic crude culture filtrate obtained from three ruminant dung isolates, Bacillus safensis M35, Bacillus altitudinis R31 and Bacillus altitudinis J208, on crude pectin containing medium possessed polygalacturonate hydrolase, pectate lyase and pectin lyase activities. Studies regarding their stability under various temperature and pH conditions revealed their mild acidic to alkaline and mesophilic nature with enzyme activity falling within the pH range 6·0-9·0 and temperature range 30-60°C. The pectinase activity was categorized as endolytic as it brought about ~50% reduction in relative viscosity of pectic polymer within initial 10 min of incubation. Synergism of pectinase activity with crude xylanase activities and/or commercial cellulase was clearly demonstrated as ~1·6 to ~1·9-fold increase in agrowaste biomass saccharification was obtained confirming the role of pectinases as accessory enzymes.
Synergism of the broad-spectrum endopectinase activity obtained from three Bacillus isolates with accessory crude xylanases from the same isolates and commercial cellulase enhanced the agrowaste saccharification and confirmed the accessory role of crude pectinase as they formed an efficient enzyme cocktail functioning in a contributive manner for improvement of agrowaste biomass saccharification.
Mesophilic crude endopectinases obtained from Bacillus spp. isolated from ruminant dung possessed activity in broad pH and temperature ranges as well as broad substrate specificity. Moreover, their synergism with crude xylanase and Primfast 200 cellulase demonstrated the potential to form efficient enzyme cocktail for application in plant biomass saccharification process.
本研究旨在评估 3 株瘤胃粪便来源芽孢杆菌粗果胶酶活性的理化性质，并研究其与同属芽孢杆菌粗木聚糖酶和商业纤维素酶的协同作用，以评估其在提高生物质糖化中的辅助作用。
从 3 株瘤胃粪便分离株芽孢杆菌（Bacillus safensis M35、Bacillus altitudinis R31 和 Bacillus altitudinis J208）的粗培养滤液中获得的果胶酶粗培养滤液，在含有粗果胶的培养基上具有聚半乳糖醛酸水解酶、果胶裂解酶和果胶裂解酶活性。研究表明，它们在各种温度和 pH 条件下的稳定性，其性质为偏酸性到碱性和中温，酶活性在 pH6.0-9.0 和温度 30-60°C 范围内。果胶酶活性被归类为内切酶，因为它在最初 10 分钟的孵育时间内使果胶聚合物的相对粘度降低了约 50%。与粗木聚糖酶活性和/或商业纤维素酶协同作用的果胶酶活性得到了明确证明，因为获得了约 1.6 至 1.9 倍的农业废弃物生物质糖化增加，证实了果胶酶作为辅助酶的作用。
从 3 株芽孢杆菌分离株获得的广谱内切果胶酶活性与同分离株的辅助粗木聚糖酶和商业纤维素酶的协同作用，增强了农业废弃物的糖化作用，并证实了粗果胶酶的辅助作用，因为它们形成了一种有效的酶混合物，以协同方式提高农业废弃物生物质的糖化作用。
从瘤胃粪便中分离得到的中温粗内切果胶酶具有较宽的 pH 和温度范围以及较宽的底物特异性。此外，它们与粗木聚糖酶和 Primfast 200 纤维素酶的协同作用表明，它们有可能形成有效的酶混合物，用于植物生物质糖化过程。
