Solid-state relaxation NMR dataset for a water-soluble β-(1→3, 1→6)-glucan from Aureobasidium pullulans and schizophyllan from Schizophyllum commune

We report the solid-state nuclear magnetic resonance (NMR) relaxation dataset for a triple helix and a random structure of water-soluble Aureobasidium pullulans β-(1→3, 1→6)-d-glucan (APG) and those of schizophyllan from Schizophyllum commune (SPG), obtained by the Bruker BioSpin 500 MHz NMR spectrometer. These data include solid-state proton spin-lattice relaxation in the rotating frame (T1ρH) and 13C spin-lattice relaxation (T1C) of these two β-(1→3, 1→6)-glucans, which are related to the subject of article in International Journal of Biological Macromolecules, entitled “Characterization of the secondary structure and order–disorder transition of a β-(1→3, 1→6)-glucan from Aureobasidium pullulans” [1]. Data can help to investigate the structural characterization of the structural polysaccharides.


Data
The presented data include the T 1rH and T 1C relaxation NMR data of a triple helix and a random structure of APG and those of SPG. 13 C NMR spectra of triple helix and a random structure of APG and those of SPG acquired by inserting 9 1 H spin-lock times that range from 0 to 15 ms during the T 1rH experiments (Figs. S1eS4), and the 13 C peaks were integrated for the following regions: C1 (110e96 ppm), C3 of the (1/3)-b-glucosyl main-chain (96e83 ppm), C6 (66e56 ppm), and other carbon resonances (83e66 ppm). The resulting integration values for each region as functions of 1 H spin-lock time are summarized in Table 1, which were fitted to the following mono-exponential function: where I t is the measured integral value at 1 H spin-lock time t and I 0 is the initial intensity (t ¼ 0) of the 13 C magnetization. The T 1rH values for the four 13 C region of each sample could be determined by the fitting curves [1]. A series of 13 C NMR spectra for a triple helix and a random structure of APG and those of SPG recorded with 10 relaxation delays that range from 0 to 60 s during the T 1C experiments (Figs. S5eS8). As described for the T 1rH experiments, the four spectral regions were integrated (Table 2), and the   Specifications Table   Subject Polymers Value of the Data The dataset is useful to characterize and understand the higher order structure of structural polysaccharides. The dataset can be useful to researchers involved in the application of solid-state NMR in polymer chemistry and structural biology.
The dataset can be used as comparison in studies investigating the structural characterization of the other b-(1/3, 1/6)glucans in the cell walls of cereals, bacteria, and fungi, with significantly differing physicochemical properties dependent on source.
To the best of our knowledge, this is the first published NMR relaxation dataset on Aureobasidium pullulans b-(1/3,

1/6)-glucan
The dataset would serve as a new analytical protocol for characterizing the formation of higher order structures of structural polysaccharides.
resulting integration values for each region as functions of 13 C relaxation delay were fitted to the following mono-exponential function: where I t and I 0 are defined as for Eq. (1). The T 1C values for the four 13 C regions for each sample could be determined by the fitting curves [1].

Experimental design, materials, and methods
APG was kindly provided from Itochu Sugar Co. (Japan), which was prepared according to a previously reported method [2e4]. SPG was purchased from InvivoGen (USA). Triple helical and single random coil structures of APG were prepared by dissolving 250 mg of APG in 50 mL of deionized water and DMSO, respectively, at 298 K for 3 d followed by lyophilization. In a method similar to that used to prepare the triple helical and single random coil structures of APG, lyophilization of SPG dissolved in water or DMSO for 3 d provided the triple helical and single random coil structures of SPG, respectively [1].
Solid-state T 1rH and T 1C experiments were performed at 298 K using a Bruker AVIII500 spectrometer (Bruker BioSpin GmbH, Germany) equipped with a 4 mm dual-tuned MAS probe according to methods previously reported [5,6]. To determine T 1rH values, Cross-polarization (CP)/MAS 13 C NMR spectra were recorded by inserting 1 H spin-lock times of 0.5, 1, 2, 3, 4, 8, 10, and 15 ms prior to CP, and MAS frequency, contact time, acquisition time, and repetition time were set to 10 kHz, 2 ms, 15 ms, and 4 s, respectively. The T 1rH values for the specific 13 C resonance regions were integrated to obtain the T 1rH curves, which were fitted to Eq. (1). The T 1C experiments were performed using the Torchia method [7]. The spectra were recorded at relaxation delays of 0.1, 0.5, 1, 2.5, 5, 7.5, 10, 30, and 60 s, and the specific 13 C resonance regions were integrated to obtain T 1C curves, which were fitted to Eq. (2). The chemical shifts were calibrated by assigning the value of 176.03 ppm to the carbonyl carbon of the external standard D-glycine.

Funding
This work was, in part, supported by the Japan Society for Promotion of Science (JSPS) [grant number JP16K05802] (H.K.).

Conflict of Interest
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.