3 Phycobiliproteins in Microalgae: Occurrence …
67
Soltani, N., Khavari-Nejad, R. A., Yazdi, M. T., & Shokravi, S. (2007). Growth and some metabolic
features of cyanobacterium Fischerella sp. FS18 in different combined nitrogen sources. Journal
of Science, Republic of Iran, 18, 123–128.
Soni, B., Kalavadia, B., Trivedi, U., & Madamwar, D. (2006). Extraction, purification and characterization of phycocyanin from Oscillatoria quadripunctulata—Isolated from the rocky shores
of Bet-Dwarka, Gujarat, India. Process Biochemistry, 41, 2017–2023.
Soni, B., Trivedi, U., & Madamwar, D. (2008). A novel method of single step hydrophobic interaction chromatography for the purification of phycocyanin from Phormidium fragile and its
characterization for antioxidant property. Bioresource technology, 99(1), 188–194.
Stadnichuk, I. N., & Tropin, I. V. (2017). Phycobiliproteins: Structure, functions and biotechnological applications. Applied Biochemistry and Microbiology, 53, 1–10.
Storf, M., Parbel, A., Meyer, M., Strohmann, B., Scheer, H., Deng, M. G., ... & Zhao, K. H.
(2001). Chromophore attachment to biliproteins: specificity of PecE/PecF, a lyase-isomerase for
the photoactive 31-cys-α84-phycoviolobilin chromophore of phycoerythrocyanin. Biochemistry,
40(41), 12444–12456.
Su, H.-N., Xie, B.-B., Zhang, X.-Y., Zhou, B.-C., & Zhang, Y.-Z. (2010). The supramolecular architecture, function, and regulation of thylakoid membranes in red algae: an overview. Photosynthesis
Research, 106, 73–87.
Sugishima, M., Hagiwara, Y., Zhang, X., Yoshida, T., Migita, C. T., & Fukuyama, K. (2005). Crystal
structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme.
Biochemistry, 44, 4257–4266.
Takano, H., Arai, T., Hirano, M., & Matsunaga, T. (1995). Effects of intensity and quality of light on
phycocyanin production by a marine cyanobacterium Synechococcus sp. NKBJ 042902. Applied
Microbiology and Biotechnology, 43, 1014–1018.
Tandeau de Marsac, N. (1983). Phycobilisomes and complementary chromatic adaptation in
cyanobacteria. Bulletin de L’Institut Pasteur, 81, 201–254.
Tcheruov, A. A., Minkova, K. M., Georgiev, D. I., & Houbavenska, N. B. (1993). Method for
B-phycoerythrin purification from Porphyridium cruentum. Biotechnology Techniques, 7(12),
853–858.
Tomasseli, L., Boldrini, G., & Margheri, M. C. (1997). Physiological behaviour of Arthrospira
(Spirulina) maxima during acclimation to changes in irradiance. Journal of Applied Phycology,
9, 37–43.
Tomasseli, L., Margheri, M. C., & Sacchi, A. (1995). Effects of light on pigments and photosynthetic
activity in a phycoerythrin—rich strain of Spirulina subsalsa. Aquatic Microbial Ecology, 9,
27–31.
Tsekos, I., Niell, F. X., Aguilera, J., Lopez-Fiueroa, F., & Delivopoulos, S. G. (2002). Ultrastructure
of vegetative gametophytic cells of Porphyra leucosticta (Rhodophyta) grown in red, blue and
green light. Phycological Research, 50, 251–264.
Tredici, M., Bassi, N., Prussi, M., Biondi, N., Rodolfi, L., Chini Zittelli, G., & Sampietro, G.
(2015). Energy balance of algae biomass production in a 1-ha “Green Wall Panel” plant: How to
produce algae biomass in a closed reactor achieving a high Net Energy Ratio. Applied Energy,
154, 1103–1111.
Tyagi, R., Srinivas, G., Vyas, D., Kumar, A., & Kumar, H. D. (1992). Differential effects of ultraviolet
–b radiation on certain metabolic processes in a chromatically adapting Nostoc sp. Photochemistry
and Photobiology, 55, 401–407.
Unno, M., Ishikawa-Suto, K., Kusaka, K., Tamada, T., Hagiwara, Y., Sugishima, M., et al.
(2015). Insights into the proton transfer mechanism of a bilin reductase PcyA following neutron
crystallography. Journal of the American Chemical Society, 137, 5452–5460.
Vaishampayan, A., Sinha, R. P., Häder, D.-P., Dey, T., Gupta, A. K., Bhan, U., & Rao. A, L. (2001).
Cyanobacterial biofertilizers in rice agriculture. The Botanical Review, 67, 453–516.
Vásquez-Suárez, A., Lobos-González, F., Cronshaw, A., Sepúlveda-Ugarte, J., Figueroa, M.,
Dagnino-Leone, J., et al. (2018). The γ33 subunit of R-phycoerythrin from Gracilaria chilensis
has a typical double linked phycourobilin similar to γ subunit. PLoS ONE, 13, e0195656.
67
Soltani, N., Khavari-Nejad, R. A., Yazdi, M. T., & Shokravi, S. (2007). Growth and some metabolic
features of cyanobacterium Fischerella sp. FS18 in different combined nitrogen sources. Journal
of Science, Republic of Iran, 18, 123–128.
Soni, B., Kalavadia, B., Trivedi, U., & Madamwar, D. (2006). Extraction, purification and characterization of phycocyanin from Oscillatoria quadripunctulata—Isolated from the rocky shores
of Bet-Dwarka, Gujarat, India. Process Biochemistry, 41, 2017–2023.
Soni, B., Trivedi, U., & Madamwar, D. (2008). A novel method of single step hydrophobic interaction chromatography for the purification of phycocyanin from Phormidium fragile and its
characterization for antioxidant property. Bioresource technology, 99(1), 188–194.
Stadnichuk, I. N., & Tropin, I. V. (2017). Phycobiliproteins: Structure, functions and biotechnological applications. Applied Biochemistry and Microbiology, 53, 1–10.
Storf, M., Parbel, A., Meyer, M., Strohmann, B., Scheer, H., Deng, M. G., ... & Zhao, K. H.
(2001). Chromophore attachment to biliproteins: specificity of PecE/PecF, a lyase-isomerase for
the photoactive 31-cys-α84-phycoviolobilin chromophore of phycoerythrocyanin. Biochemistry,
40(41), 12444–12456.
Su, H.-N., Xie, B.-B., Zhang, X.-Y., Zhou, B.-C., & Zhang, Y.-Z. (2010). The supramolecular architecture, function, and regulation of thylakoid membranes in red algae: an overview. Photosynthesis
Research, 106, 73–87.
Sugishima, M., Hagiwara, Y., Zhang, X., Yoshida, T., Migita, C. T., & Fukuyama, K. (2005). Crystal
structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme.
Biochemistry, 44, 4257–4266.
Takano, H., Arai, T., Hirano, M., & Matsunaga, T. (1995). Effects of intensity and quality of light on
phycocyanin production by a marine cyanobacterium Synechococcus sp. NKBJ 042902. Applied
Microbiology and Biotechnology, 43, 1014–1018.
Tandeau de Marsac, N. (1983). Phycobilisomes and complementary chromatic adaptation in
cyanobacteria. Bulletin de L’Institut Pasteur, 81, 201–254.
Tcheruov, A. A., Minkova, K. M., Georgiev, D. I., & Houbavenska, N. B. (1993). Method for
B-phycoerythrin purification from Porphyridium cruentum. Biotechnology Techniques, 7(12),
853–858.
Tomasseli, L., Boldrini, G., & Margheri, M. C. (1997). Physiological behaviour of Arthrospira
(Spirulina) maxima during acclimation to changes in irradiance. Journal of Applied Phycology,
9, 37–43.
Tomasseli, L., Margheri, M. C., & Sacchi, A. (1995). Effects of light on pigments and photosynthetic
activity in a phycoerythrin—rich strain of Spirulina subsalsa. Aquatic Microbial Ecology, 9,
27–31.
Tsekos, I., Niell, F. X., Aguilera, J., Lopez-Fiueroa, F., & Delivopoulos, S. G. (2002). Ultrastructure
of vegetative gametophytic cells of Porphyra leucosticta (Rhodophyta) grown in red, blue and
green light. Phycological Research, 50, 251–264.
Tredici, M., Bassi, N., Prussi, M., Biondi, N., Rodolfi, L., Chini Zittelli, G., & Sampietro, G.
(2015). Energy balance of algae biomass production in a 1-ha “Green Wall Panel” plant: How to
produce algae biomass in a closed reactor achieving a high Net Energy Ratio. Applied Energy,
154, 1103–1111.
Tyagi, R., Srinivas, G., Vyas, D., Kumar, A., & Kumar, H. D. (1992). Differential effects of ultraviolet
–b radiation on certain metabolic processes in a chromatically adapting Nostoc sp. Photochemistry
and Photobiology, 55, 401–407.
Unno, M., Ishikawa-Suto, K., Kusaka, K., Tamada, T., Hagiwara, Y., Sugishima, M., et al.
(2015). Insights into the proton transfer mechanism of a bilin reductase PcyA following neutron
crystallography. Journal of the American Chemical Society, 137, 5452–5460.
Vaishampayan, A., Sinha, R. P., Häder, D.-P., Dey, T., Gupta, A. K., Bhan, U., & Rao. A, L. (2001).
Cyanobacterial biofertilizers in rice agriculture. The Botanical Review, 67, 453–516.
Vásquez-Suárez, A., Lobos-González, F., Cronshaw, A., Sepúlveda-Ugarte, J., Figueroa, M.,
Dagnino-Leone, J., et al. (2018). The γ33 subunit of R-phycoerythrin from Gracilaria chilensis
has a typical double linked phycourobilin similar to γ subunit. PLoS ONE, 13, e0195656.