2005
DOI: 10.1007/s10930-004-1514-8
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Effect of Glycosylation on the Catalytic and Conformational Stability of Homologous α-Amylases

Abstract: A thermostable alpha-amylase from B. licheniformis (BLA) and a mesophilic amylase from B. amyloliquefaciens (BAA) were covalently coupled to oxidized synthetic sucrose polymers (OSP400 and OSP70) and polyglutaraldehyde (PGA) by reductive alkylation to study the effect of neoglycosylation on the activity, kinetic and thermodynamic stability. The catalytic efficiency of the modified enzymes was comparable to that of the native enzyme. Covalent coupling decreased the rate of inactivation at all the temperatures s… Show more

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Cited by 16 publications
(8 citation statements)
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“…Moreover, it is commonly observed that the glycosylated protein has an increased thermal stability compared to the nonglycosylated form and that it is less susceptible to proteolysis [24–26]. The increased thermal stability, typically in the order of 4 °C [27,28], is generally explained by the fact that the carbohydrate moiety increases the chain stiffness near its attachment site. As a result, the entropy gain upon unfolding is reduced and the native‐unfolded equilibrium is shifted slightly to the left [24–26].…”
Section: Discussionmentioning
confidence: 99%
“…Moreover, it is commonly observed that the glycosylated protein has an increased thermal stability compared to the nonglycosylated form and that it is less susceptible to proteolysis [24–26]. The increased thermal stability, typically in the order of 4 °C [27,28], is generally explained by the fact that the carbohydrate moiety increases the chain stiffness near its attachment site. As a result, the entropy gain upon unfolding is reduced and the native‐unfolded equilibrium is shifted slightly to the left [24–26].…”
Section: Discussionmentioning
confidence: 99%
“…By far, the most employed strategy to prepare neoglycoenzymes is the covalent cross-linking with periodate-oxidized oligo- and polysaccharide via reductive alkylation (Figure ). , ,,,, Meta periodate ion cleaves C–C bonds that possess adjacent hydroxyl groups by oxidation to highly reactive aldehydes. This approach permits one to control the oxidation level of the carbohydrate by manipulating the m -NaIO 4 /monosaccharide ratio .…”
Section: Strategies For Preparing Artificial Glycoenzymesmentioning
confidence: 99%
“…Sodium borohydride is commonly employed for these reductive alkylation processes, ,,,,,,,,, although it reduces both the imine and the aldehyde groups, thereby limiting the number of attachments between the enzyme and the activated carbohydrate. Sodium cyanoborohydride, a mild reducing agent that does not reduce aldehyde groups, has been also used. , ,,, However, the toxicity associated with the cyanide as well as the inhibitory effect that reactive aldehyde groups cause on the catalytic activity of several enzymes are the main drawbacks of NaBH 3 CN. The latter can be solved by using sequential reduction steps with NaBH 3 CN and NaBH 4 . Borane–pyridine complex has been also employed as reducing agent for preparing neoglycoenzymes via reductive alkylation with periodate-oxidized carbohydrates …”
Section: Strategies For Preparing Artificial Glycoenzymesmentioning
confidence: 99%
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“…For the purpose of comparing the gains in thermal stability obtained for each immobilized catalyst, the stabilization factor (SF)-ratio between the half-lives, t 1/2 , of the immobilized and free enzymes [37][38][39]-was computed, when possible. If the deactivation is assumed to be exclusively thermal and obeying a first-order kinetics (Eq.…”
Section: Hydrolysis Assaysmentioning
confidence: 99%