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Activity and expression of banana starch phosphorylases during fruit development and ripening
Abstract
Two main forms of starch phosphorylase (EC 2.4.1.1) were identified and purified from banana (Musa acuminata Colla. cv. Nanicão) fruit. One of them, designated phosphorylase I, had a native molecular weight of 155 kDa and subunit of 90 kDa, a high affinity towards branched glucans and an isoelectric point around 5.0. The other, phosphorylase II, eluted at a higher salt concentration from the anion exchanger, had a low affinity towards branched glucans, a native molecular weight of 290 kDa and subunit of 112 kDa. Kinetic studies showed that both forms had typical hyperbolic curves for orthophosphate (Pi) and glucose-1-phosphate, and that they could not react with substrates with a blocked reducing end or alpha-1,6 glucosidic bonds. Antibodies prepared against the purified type-II form and cross-reacting with the type-I form showed that there was an increase in protein content during development and ripening of the fruit. The changes in protein level were parallel to those of phosphorylase activity, in both the phosphorolytic and synthetic directions. Considering the kinetics, indicating that starch phosphorylases are not under allosteric control, it can be argued that protein synthesis makes a contribution to regulating phosphorylase activity in banana fruit and that hormones, like gibberellic acid and indole-3-acetic acid, may play a regulating role. For the first time, starch phosphorylases isoforms were detected as starch-granule-associated proteins by immunostaining of SDS-PAGE gels.
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Da Mota et al. extracted two different forms of phosphorylase from unripe banana (Musa acuminata Colla. cv. Nanicão) fruits-phosphorylase I and phosphorylase II.
“Da Mota et al. [59] extracted two different forms of phosphorylase from unripe banana ( Musa acuminata Colla. cv. Nanic ã o) fruits-phosphorylase I and phosphorylase II.”
From Potential Valorization of Banana Production Waste in Developing Countries: Bio-Engineering Aspects (2024) · cites this paper as [59]
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Potential Valorization of Banana Production Waste in Developing Countries: Bio-Engineering Aspects
Waraczewski, R., & Sołowiej, B. G. (2024) · Fibers · doi:10.3390/fib12090072 · Cited by 10
Metadata
- Authors
- da Mota, R., Cordenunsi, B., do Nascimento, J., Purgatto, E., Rosseto, M., & Lajolo, F.
- Affiliations
- Universidade de São Paulo (BR)
- Corresponding author
- Lajolo, Franco
- Venue
- Planta
- Published
- 2002-12-01
- Volume
- 216
- Issue
- 2
- Pages
- 325-333
- ISSN
- 0032-0935 (ISSN-L)
- OpenAlex
- W2070643927
- Cited by
- 59
- References
- 28
- Citations by year
- 2024: 4 · 2023: 1 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 4 · 2018: 2 · 2017: 5 · 2016: 4 · 2015: 2 · 2014: 2 · 2013: 5 · 2012: 4
- FWCI
- 2.11
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Planta (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fundação de Amparo à Pesquisa do Estado de São Paulo
- Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Postharvest Quality and Shelf Life Management
- Health Sciences › Nursing › Nutrition and Dietetics › Food composition and properties
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Banana Cultivation and Research
- Keywords
- starch phosphorylase, banana fruit, fruit development, fruit ripening, enzyme kinetics, branched glucan, protein synthesis regulation, gibberellic acid, indole-3-acetic acid, allosteric regulation, Musa acuminata
- MeSH terms
- Fruit, Gibberellins, Glucans, Glucosephosphates, Indoleacetic Acids, Isoenzymes, Kinetics, Molecular Weight, Phosphates, Plant Growth Regulators, Starch, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Gene Expression Regulation, Developmental, Starch Phosphorylase, Musa
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