Abstract
Abstract In this experiment, optimum experimental conditions for the enzymatic hydrolysis of grass at different stages of growth were obtained by using the Taguchi methodology. Rye grass silage and three growth stages of Italian rye grass samples were used to determine optimum hydrolysis conditions. Five factors (pretreatment, enzyme composition, incubation temperature, pretreatment time, pH) influencing the hydrolysis process were studied at the individual and interactive levels. All selected experimental factors influenced the hydrolysis of grass. At the individual level, pretreatment of grass with NaOH and enzyme composition had the greatest influence (75% and 14.7% of the variance respectively) on enzymatic hydrolysis. Incubation temperature, pretreatment time and pH had influences of 8.1%, 2.2% and 0.055%, respectively. pH and incubation temperature had the most significant interaction effect (65.6%) on enzymatic hydrolysis. The factors with the least individual influence had the most significant interaction effect on enzymatic hydrolysis. Hydrolysis was improved when optimised conditions were applied to different growth stages of Italian rye grass.
Highlights
Eukaryotic cells are inhomogeneously crowded with biological macromolecules and often contain numerous cellular bodies, including proteinaceous membrane-less organelles (PMLOs)
They are formed as a result of highly regulated and reversible liquid-liquid demixing phase separation and represent condensed liquid droplets, which are invariantly enriched in intrinsically disordered proteins
Phase transitions leading to the formation of PMLOs are controlled by many factors, including the concentrations of the involved IDPs, their conformational flexibility, some sequence peculiarities that define their flexible multivalency, the ability to be engaged in specific but weak interactions, posttranslational modifications, and the peculiarities of the local environment, such as temperature, pH, salt concentration, and osmolarity
Summary
Protein science was revolutionized by recognizing the importance of macromolecular crowding for protein structure and function [1,2,3,4], and by the discovery that. It is known that formation of IBs is a reversible process, since misfolded and aggregated proteins can be spontaneously released from IBs, leading to the almost complete IB disintegration and to the appearance of soluble and properly folded proteins [55]
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