Immobilization of β-cyclodextrin glycosyltransferase on gelatin enhances β-cyclodextrin production

Distribution of Aromatic Amino Acid Residues in Substrate-Binding Regions Modulates Substrate Specificity of Microbial Debranching Enzymes

“…Starch is the second largest renewable resource in nature and is considered one of the most important raw materials for the manufacture of foods, chemicals, and medicines. − In the sugar industry, starch is also a pivotal raw material to produce sugars by diverse amylolytic enzymes. , For example, starch can be enzymatically hydrolyzed into glucose and maltose by glucoamylase (EC 3.2.1.3) and β-amylase (EC 3.2.1.2), respectively . Besides, starch can be also applied to produce cyclodextrin and oligosaccharides through the action of cyclodextrin glycosyltransferase (EC 2.4.1.19) and maltooligosaccharide-forming amylases (EC 3.2.1.-), respectively. − Although various amylolytic enzymes have been used in starch processing, most of them are very expensive or inefficient in starch conversion . The majority of α-amylase, β-amylase, and α-glucosidase enzymes can hydrolyze α-1,4-glucosidic linkages in starch but have low activities for α-1,6-linkages, , resulting in a low overall conversion rate of starch material and large amounts of byproducts. , Therefore, eliminating α-1,6 branches by debranching enzymes (DBEs) during starch degradation is a critical and well-established approach to facilitate starch hydrolysis and improve production efficiency …”

Immobilization of Cyclodextrin glycosyltransferase onto three dimensional‐ hydrophobic and two dimensional‐ hydrophilic supports: A comparative study

“…The total CDs productivities per gram of support were 1.22 mg.min −1 for Si‐SH (α:β:γ ratio 1.4:1.5:1) and 1.56 mg.min −1 for Si‐NH (α:β:γ ratio 3.3:3:1). [ 6 ] Also, in order to facilitate unrestrained access to the active site on immobilized CGTase, covalent attachment via inclusion of 3‐aminopropyltrimethoxysilane (APTMS) as a spacer arm was studied, which led to an activity recovery of 73%. [ 45 ] In another study, CDs yield of 40% CD was achieved after 1.2 h retention time, using CGTase from B. macerans immobilized on Amberite IRA 900 with 10% (w/w) partially cyclized starch at 50°C.…”

“…Comparing the results in the current work to those reported in literature using CGTase immobilized on other supports, for example, using for Si-SH (α:β:γ ratio 1.4:1.5:1) and 1.56 mg.min −1 for Si-NH (α:β:γ ratio 3.3:3:1). [6] Also, in order to facilitate unrestrained access to the active site on immobilized CGTase, covalent attachment via inclusion of 3aminopropyltrimethoxysilane (APTMS) as a spacer arm was studied, which led to an activity recovery of 73%. [45] In another study, CDs yield of 40% CD was achieved after 1.2 h retention time, using CGTase from B. macerans immobilized on Amberite IRA 900 with 10% (w/w) partially cyclized starch at 50 • C. [46] Furthermore, improved yield of CDs (43%) was obtained after 3 h with an α:β:γ mass ratio of 1.5:2:1 at enzyme loading of 5.0 U per g starch, using post-modified CGTase to form crosslinked enzyme aggregates (CLEAs).…”

“…[3] For CGTase immobilization, various porous three dimensional (3-D) supports have been tested, including Eupergit C, [4] polyvinylidene difluoride (PVDF), [5] and silica. [6] Different methods of immobilization, including adsorption, covalent binding, and entrapment have likewise been reported. [7] The reason behind selecting porous threedimensional support is high porosity, allowing increased loading of the enzyme.…”

Novel biotechnological approaches to improving aromas and flavors of legume‐derived food products

“…CDs are also known to bind to “hydrophobic” amino acids responsible for bitterness and to active sites of some enzymes, thereby inhibiting their activities (Fenyvesi et al, 2016). Interestingly, CDs can, particularly, inhibit CGTases, which catalyze their production (Chen et al, 2022; Leemhuis et al, 2003). Formation of CD‐lipid and CD‐carbohydrate (e.g., CD‐starch) complexes was reported as well (Fenyvesi et al, 2016).…”