Application of cyclodextrinase in non‐complexant production of γ‐cyclodextrin

Abstract

The production of γ‐cyclodextrin usually includes the utilization of organic complexants. However, the non‐complexant production of γ‐cyclodextrin is always being explored due to the defects of organic complexants. However, in non‐complexant production, the separation of γ‐cyclodextrin from α‐ and β‐cyclodextrin is still a challenge. Here, the selective hydrolysis ability of a cyclodextrinase designated PpCD (cyclodextrinase from Palaeococcus pacificus) on α‐cyclodextrin, β‐cyclodextrin, and γ‐cyclodextrin was proved. The kcat/Km values of PpCD for α‐cyclodextrin and β‐cyclodextrin were roughly 12‐fold and 5‐fold higher than that of γ‐cyclodextrin. It was proved that PpCD had selective hydrolysis ability and its γ‐cyclodextrin purification performance was apparent on various simulated cyclodextrin mixtures with reported proportions derived from different CGTases. Besides, the hydrolysis temperature was optimized and it could be seen that 85°C was appropriate for the production of γ‐cyclodextrin. In addition, the production of γ‐cyclodextrin was achieved by using PpCD in the γ‐CGTase reaction products.

Enantioselective Labeling of Zebrafish for D-Phenylalanine Based on Graphene-Based Nanoplatform

“…Chemical functionalization procedure was also fully investigated by means of fourier infrared spectrum (FT-IR). Seen from the FT-IR analysis in Figure S2A, obvious conversion was demonstrated: the distinct peaks for native γ-CD were also found in γ-CD-GO around 1050 to 1346 cm −1 , related to the C-O-C bond asymmetric stretching vibration [49,50]. More important, the stretching vibration of -COOH in GO at 1729 cm −1 was redshifted to 1680 cm −1 in γ-CD-GO, attributed to a dehydration reaction between carboxyl groups and amine groups to generate a covalent bond of amide.…”

A Cyclodextrin-Based Controlled Release System in the Simulation of In Vitro Small Intestine

“…One unit of β-CGTase activity was defined as the amount of enzyme used for producing 1 µmol of β-CD per minute under the assay conditions. The activity of AG was analyzed in PBS (20 mM, pH 6.0) using 1% (w/v) soluble starch as substrate at 45 • C for 10 min, according to the 3,5-dinitrosalicylic acid (DNS) method [34,35]. The reaction mixture contained the enzyme (0.17 mg/mL), and the final volume was 1 mL.…”