Activation and stabilization of 10 starch-degrading enzymes by Triton X-100, polyethylene glycols, and polyvinyl alcohols

Yoon, Seung-Heon; Robyt, John F.

doi:10.1016/j.enzmictec.2005.04.002

Cited by 59 publications

(26 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The enzymes that can withstand extreme conditions can be isolated from extremophiles. The stabilization can be achieved by the addition of additives like substrates, products, inhibitors, cofactors, metal ions, proteins, sugars and natural or synthetic polymers [1][2][3][4][5]. The use of enzymes for industrial purposes usually depends on their stability during isolation, purifi cation and storage [3].…”

Section: Introductionmentioning

confidence: 99%

Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-640

2010

View full text Add to dashboard Cite

Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-640 with various stabilizers at different temperatures was studied. Dextransucrase was stable at lower temperatures (10-30°C) and lost the activity at above 30°C. The salts such as CaCl 2 , CoCl 2 and MgCl 2 enhanced the dextransucrase activity. A 22% higher dextransucrase activity was obtained by 4 mM CoCl 2 . The dextransucrase activity was lost by 50% at 1 mM EDTA. Urea denatured the enzyme and caused 45%, 90% and 98% loss of activity in 30 min when treated with 1 M, 3 M, and 5 M urea concentrations, respectively. Amongst the stabilizers Tween 80, glycerol, PEG-8000, dextran (500 kDa) and glutaraldehyde, Tween 80 provided the maximum stability at 30°C. In the presence of Tween 80 the enzyme lost only 8% activity at 30°C in 20 h but, it lost 65% of activity with out any stabilizer. The enzyme lost 92% of activity with in 4 days at 30°C and lost only 25% of activity at -20°C after 14 days.

show abstract

Section: Introductionmentioning

confidence: 99%

Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-640

2010

View full text Add to dashboard Cite

show abstract

“…Interestingly, it has previously been shown that this non-ionic detergent activates and stabilizes porcine pancreatic AAMYs. The activation and stabilization of 10 starch-degrading enzymes by Triton X-100 are thought to occur through the binding of the detergent to the enzymes, which promote an optimally folded and compact barrel motif structure and produce the maximum possible amount of activity [16].…”

Section: Discussionmentioning

confidence: 99%

Characterization of the activity and stability of amylase from saliva and detergent: Laboratory practicals for studying the activity and stability of amylase from saliva and various commercial detergents

Valls

Rojas

Pujadas

et al. 2012

Biochem Molecular Bio Educ

View full text Add to dashboard Cite

This article presents two integrated laboratory exercises intended to show students the role of α‐amylases (AAMYs) in saliva and detergents. These laboratory practicals are based on the determination of the enzymatic activity of amylase from saliva and different detergents using the Phadebas test (quantitative) and the Lugol test (qualitative) under different conditions (e.g. variations in temperature and alkalinity). This work also proposes the study of enzyme stability in the presence of several surfactants and oxidizing agents using the same technical approach. The proposed laboratory exercises promote the understanding of the physiological function of this enzyme and the biotechnological applications of AAMYs in the detergent industry. The exercises also promote the understanding that the enzymatic stability and performance are dependent on the organism of origin, and if necessary, these properties could be modified by genetic engineering. In addition, this article reinforces the development of laboratory skills, problem‐solving capabilities, and the ability to write a laboratory report. The exercises are proposed primarily as an undergraduate project for advanced students in the biochemical and biotechnological sciences. These laboratory practicals are complementary to the previously published BAMBED article (Biochemistry and Molecular Biology Education Vol. 39, No. 4, pp. 280–290, 2011) on detergent proteases.

show abstract

“…In addition, Ooshima et al (1986) demonstrated that surfactants prevent the adsorption of endoglucanase from cellulose and change the adsorption balance of endoglucanase and exoglucanase, thereby increasing the concentration of endoglucanase in the liquid phase. Surfactants effectively improve enzyme activity during hydrolysis by binding to the tertiary structure of the enzyme protein (Yoon and Robyt, 2005). Okino et al (2013) showed that Tween-80 can improve and stabilize not only cellulase enzyme production but also cellulose hydrolysis.…”

Section: Introductionmentioning

confidence: 99%

Enhanced enzymatic xylose/cellulose fractionation from alkaline liquor-pretreated corn cob by surfactant addition and separate fermentation to bioethanol

Chen¹,

Zhang²,

Zhang³

et al. 2014

Turk J Biol

View full text Add to dashboard Cite

Xylanase xylose/cellulose fractionation can efficiently improve the utilization of xylose and cellulose. Improvement of xylanase performance during hemicellulose hydrolysis can increase xylose/cellulose fractionation efficiency. To utilize xylose and cellulose efficiently, an enzymatic xylose/cellulose fractionation and a separate fermentation bioethanol process were performed. Alkaline liquorpretreated corn cob was subjected to xylose/cellulose fractionation with xylanase in the presence or absence of the following mixed surfactants: polyoxyethylene(20)-sorbitan-monooleate (0.15% v/v), polyethylene glycol 6000 (0.15% w/v), bovine serum albumin (0.15% w/v), and rhamnolipid (0.005% v/v). The hemicellulose hydrolysis yield (HHY) in the presence of mixed surfactants was 70.5%, which was 66% higher than that of the control (no surfactants added). Optimization of other hydrolysis conditions, such as pH, temperature, liquid-to-solid ratio, xylanase loading, and incubation time, increased the HHY to 86.62%. The xylose in the enzymatic hydrolysate was fermented to ethanol by Candida shehatae, and the cellulose remaining in the solid residues was converted to ethanol by simultaneous saccharification and fermentation with Saccharomyces cerevisiae. In total, 40.67% of the hemicellulose and 76.14% of the cellulose in the raw corn cob was converted to ethanol.

show abstract

Activation and stabilization of 10 starch-degrading enzymes by Triton X-100, polyethylene glycols, and polyvinyl alcohols

Cited by 59 publications

References 22 publications

Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-640

Stabilization of dextransucrase from Leuconostoc mesenteroides NRRL B-640

Characterization of the activity and stability of amylase from saliva and detergent: Laboratory practicals for studying the activity and stability of amylase from saliva and various commercial detergents

Enhanced enzymatic xylose/cellulose fractionation from alkaline liquor-pretreated corn cob by surfactant addition and separate fermentation to bioethanol

Contact Info

Product

Resources

About