Synergistic Effect of Moderate Steam Explosion Pretreatment and Bovine Serum Albumin Addition for Enhancing Enzymatic Hydrolysis of Poplar

2021 ◽  
Author(s):  
Xiaodi Wang ◽  
Dayong Ding ◽  
Zhong Liu ◽  
Jinru Cheng ◽  
Xin Li ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Bovine Serum Albumin ◽  
Synergistic Effect ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Steam Explosion ◽  
Steam Explosion Pretreatment ◽  
Hydrolysis Of

scholarly journals Comparison of the Interaction Modes Between Cellulase and Bovine Serum Albumin /Lignosulfonate /Polyethylene Glycol in Promoting Lignocellulose Saccharification

2021 ◽  
Author(s):  
Peipei Wang ◽  
Tian Liu ◽  
Jiaqi Guo ◽  
Yongcan Jin ◽  
Huining Xiao ◽  
...  
Keyword(s):  
Polyethylene Glycol ◽  
Enzymatic Hydrolysis ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Enzymatic System ◽  
Promoting Effect ◽  
Pure Cellulose ◽  
Hydrolysis Of ◽  
Nonproductive Binding

Abstract Background: Bovine serum albumin (BSA), polyethylene glycol (PEG) and lignosulfonate (LS) have been extensively employed as synergistic agents in lignocellulose saccharification, albeit it has not been fully understood how they interact with enzymes from the perspectives of molecular interactions. Herein, we attempted to unveil the promotion mechanisms of BSA, PEG and LS for lignocellulose saccharification from the perspective of their respective interaction with cellulase using Quartz Crystal Microbalance with Dissipation monitoring (QCM-D), Surface Plasmon Resonance (SPR), and Small Angle X-ray Scattering (SAXS) to investigate their respective interaction and the complex formation. In the meanwhile, we compared the effects of adding these additives into the enzymatic hydrolysis of pure cellulose (Avicel) and green liquor-pretreated lignocellulose (GL).Results: The results showed that BSA and LS could bind to cellulase to form complexes, whereas PEG did not. However, PEG had a high affinity to lignin or lignin derivatives. In term for Avicel and GL substrates, the results showed that BSA and PEG promoted the enzymatic hydrolysis of both substrates, while LS had a promoting effect for GL only and inhibited some extent for Avicel. Conclusions: This study showed that synergistic agents of LS, BSA, and PEG have different interaction modes with cellulase. BSA and LS form complexes with cellulase and the formed complexes prevent from nonproductive binding by residue lignin; whereas PEG prevents from nonproductive binding by forming a thin layer on residue lignin which actually serve as steric hindrance. This investigation will help us to understand the sophisticated interactions among the components in the complicated enzymatic system, especially the interactions between enzymes and synergistic agents. It will be helpful in the design and utilization of synergistic additives in the lignocellulose biorefinery process as well.

Synergy of hemicelluloses removal and bovine serum albumin blocking of lignin for enhanced enzymatic hydrolysis

2019 ◽  
Vol 273 ◽  
pp. 231-236 ◽  
Author(s):  
Dayong Ding ◽  
Pengyun Li ◽  
Xueming Zhang ◽  
Shri Ramaswamy ◽  
Feng Xu
Keyword(s):  
Enzymatic Hydrolysis ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

scholarly journals Effects of weak bases on the degradation of endogenous and exogenous proteins by rat yolk sacs

1980 ◽  
Vol 188 (3) ◽  
pp. 895-903 ◽  
Author(s):  
G Livesey ◽  
K E Williams ◽  
S E Knowles ◽  
F J Ballard
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Normal Values ◽  
Free Medium ◽  
Weak Base ◽  
Weak Bases ◽  
Endogenous Proteins ◽  
Hydrolysis Of

In rat yolk sacs incubated in vitro, the rates of degradation of endogenous [3H]leucine-labelled proteins and of pinocytically ingested 125I-labelled bovine serum albumin were both decreased in the presence of either ammonium, methylammonium or ethylammonium ions (0-20 mM) or much lower concentrations of chloroquine (0-500 microM). These effects were also accompanied by an inhibition of pinocytosis, as measured by the rate of uptake of 125I-labelled polyvinylpyrrolidone, and by a fall in the [ATP]/[ADP] ratio within the tissue. Re-incubation in inhibitor-free medium of yolk sacs previously exposed to a weak base restored pinocytic and proteolytic capacities, except for tissues exposed to chloroquine at concentrations above 0.1 mM (these appeared to be cytotoxic); an attendent rise in [ATP]/[ADP] ratios to near normal values was also observed. Weak bases, at concentrations that fully arrested the breakdown of 125I-labelled albumin, failed to inhibit by more than 45% the degradation of [3H]leucine-labelled endogenous proteins. Since 125I-labelled bovine serum albumin has been shown to be degraded entirely intralysosomally by yolk sacs, this suggests either that the hydrolysis of endogenous proteins is shared between lysosomes and some other site or that, unlike 125I-labelled albumin, some endogenous proteins can be degraded within lysosomes at abnormally high pH.

A fluorescence turn-on probe for human (bovine) serum albumin based on the hydrolysis of a dioxaborine group promoted by proteins

2017 ◽  
Vol 53 (48) ◽  
pp. 6432-6435 ◽  
Author(s):  
Qian Sun ◽  
Weisi Wang ◽  
Zhaoyang Chen ◽  
Yuhua Yao ◽  
Weibing Zhang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
High Selectivity ◽  
Biologically Relevant ◽  
Turn On ◽  
Fluorescence Turn On ◽  
Hydrolysis Of

A reaction-based florescence probe CBF for serum albumin (SA) was proposed by connecting a dioxaborine unit with environment-sensitive coumarin fluorophore. CBF exhibits high selectivity and sensitivity toward SA over other biologically relevant species and has potential of detecting SA in biosamples.

Influence of Amitrole Upon Protein Metabolism in Bean Plants

Weed Science ◽  
1968 ◽  
Vol 16 (2) ◽  
pp. 222-226 ◽  
Author(s):  
John C. Brown ◽  
Mason C. Carter
Keyword(s):  
Free Radical ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Radical Formation ◽  
Bean Plants ◽  
Free Radical Formation ◽  
Synthesis Activity ◽  
Hydrolysis Of ◽  
Bean Protein

No effect was shown of 3-amino-l,2,4-triazole (amitrole) upon the incorporation of alanine or histidine into soluble protein in bean (Phaseolus vulgaris L.) hypocotyls grown in darkness. The metabolic derivative of amitrole, β-(3-amino-1,2,4-triazolyl-l-)α-ala-nine (hereinafter referred to as 3-ATAL), also had no effect upon histidine incorporation. Serine incorporation was increased 56% in the presence of amitrole, but this may result from a reduction of endogenous serine pools. No evidence indicates a general disruption of protein synthesis. Activity from amitrole-5-14C was readily incorporated into bean protein, but hydrolysis revealed no 3-ATAL. Most of the activity was recovered as amitrole. Amitrole in the presence of riboflavin and light attacked bovine serum albumin, probably by free radical formation. Hydrolysis of bovine serum albumin revealed mainly amitrole. Apparently, the entry of amitrole into bean protein is by free radical formation.

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