## 2 Materials and Methods
### Biochemical Composition  
#### 2.4.1 Carbohydrate, Protein and Lipid  
To determine carbohydrates, 50 mg of lyophilized biomass is dissolved in 2.5 mL of 2 N H\({}_{2}\)SO\({}_{4}\) and boiled in a 100 \({}^{\circ}\)C water bath for 3 h. Then, the sample is neutralized by adding CaCO\({}_{3}\) until there is no foam, made up with 50 mL of dH\({}_{2}\)O, and centrifuged at 4000 rpm for 5 min, using only the supernatant. Next, 0.1-0.5 mL of the sample is placed in each of five glass tubes and the remaining 1 mL is filled with dH\({}_{2}\)O. Also, 0.05 mL of phenol solution and 5 mL of sulfuric acid are added to each tube, inverted, and placed in an incubator set at 25 \({}^{\circ}\)C for 20 min. After 20 min, the OD is measured at 490 nm [28].  
To measure protein, transfer 20 mg of lyophilized biomass to a 1.7 mL tube, add 0.5 mL of RIPA lysis buffer solution (GenDEPOT, Katy, TX, USA), and sonicate for 1 h (at5 s internally). Then, incubate at 100 \({}^{\circ}\)C for 30 min and centrifuge at 4 \({}^{\circ}\)C, 11,000\(\times\)\(g\) for 15 min. Transfer 600 \(\mu\)L of the supernatant to a 5 mL tube, add four times the volume of the supernatant to the tube with a solution containing 10% (\(w/v\)) trichloroacetic acid (Sigma-Aldrich, Bengaluru, India), and incubate at \(-\)20 \({}^{\circ}\)C overnight. Divide into equal volumes in a tube and centrifuge at 18,400\(\times\)\(g\) for 15 min. Discard the supernatant, loosen the pellet with 500 \(\mu\)L of ice-cold acetone, and centrifuge again at 18,400\(\times\)\(g\) for 15 min. Discard the supernatant, add 200 \(\mu\)L of ice-cold acetone, collect in one tube, spin the centrifuge, and discard the resulting supernatant. Air dry and dissolve the sample in 2 mL of 8 M urea (Sigma-Aldrich, St. Louis, MO, USA) (pH 8.8) in 60 mM Tris-HCl (Biosesang, Yongin, Republic of Korea). Place 0, 20, 40, 60, 80, and 100 \(\mu\)L of sample in each of six glass tubes and fill the rest with dH\({}_{2}\)O. Fill with 2 mL of BCA working reagent (WR) and allow it to react for 30 min in an incubator at 37 \({}^{\circ}\)C; then, measure the OD at 562 nm [29]. All of the protein samples were quantified using Pierce BCA protein assay kits (Thermo Scientific, Waltham, MA, USA), with bovine serum albumin (BSA) (Thermo Scientific, Vilnius, Lithuania) used as the standard.  
Based on the sulfo-phospho-vanillin (SPV) method [30], 10 mg of biomass and 1 mL of Dh\({}_{2}\)O were added and sonicated. Five glass tubes were filled with 10, 20, 30, 40, and 50 \(\mu\)L of the sample, respectively, and the rest was filled with dH\({}_{2}\)O to make a total of 100 \(\mu\)L. Then, 2 mL of concentrated sulfuric acid (H\({}_{2}\)SO\({}_{4}\)) was added to each tube, and the samples were incubated at 100 \({}^{\circ}\)C for 10 min, followed by cooling on ice for 5 min. A phospho-vanillin (PV) reagent solution of 5 mL was prepared and added to the samples. The samples were shaken at 200 rpm for 15 min at 37 \({}^{\circ}\)C. Finally, the optical density (OD) was measured at 530 nm using a spectrophotometer. A calibration curve was generated using canola oil as the lipid standard at concentrations of 0, 10, 20, 30, 40, 50, 60, and 70 \(\mu\)L mL\({}^{-1}\), each measured in triplicate. The resulting regression equation was y = 0.005x \(-\) 0.0031 (R\({}^{2}\) = 0.9938), where y represents the absorbance at 530 nm and x is the lipid concentration in \(\mu\)L mL\({}^{-1}\).