Padmashree D, Srinivas M, Pooja D, Hema S, Karigar C S, Krupa S
{"title":"Extraction and Standardisation of Acid Phosphatase from the seeds of Abelmoschus esculentus (Okra)","authors":"Padmashree D, Srinivas M, Pooja D, Hema S, Karigar C S, Krupa S","doi":"10.52711/0974-4150.2024.00003","DOIUrl":null,"url":null,"abstract":"Acid phosphatase was extracted from Abelmoschus esculentus seeds at different pH levels in various buffers. The enzyme was allowed to react with p-nitrophenylphosphate which showed the highest activity in 100mM acetate buffer, pH 5.0 on the 4th day of germination. While the protein was found to be high on the 6th day. The protein content declined from the 11tn day whereas the content remained constant from the 18th day onward. The enzyme showed maximum activity while subjected to a temperature of 550C and pH 5.0, respectively. The enzyme was thermostable at 500C - 600C and pH stable at 4.0 - 5.5. The Km and Vmax values for pNPP were determined as 0.27mM and 9.09 micromoles/min respectively. In the present work, standardization of the kinetic parameters has been performed for achieving the purification and characterization of acid phosphatase which are currently underway.","PeriodicalId":8550,"journal":{"name":"Asian Journal of Research in Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2024-02-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Asian Journal of Research in Chemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.52711/0974-4150.2024.00003","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Acid phosphatase was extracted from Abelmoschus esculentus seeds at different pH levels in various buffers. The enzyme was allowed to react with p-nitrophenylphosphate which showed the highest activity in 100mM acetate buffer, pH 5.0 on the 4th day of germination. While the protein was found to be high on the 6th day. The protein content declined from the 11tn day whereas the content remained constant from the 18th day onward. The enzyme showed maximum activity while subjected to a temperature of 550C and pH 5.0, respectively. The enzyme was thermostable at 500C - 600C and pH stable at 4.0 - 5.5. The Km and Vmax values for pNPP were determined as 0.27mM and 9.09 micromoles/min respectively. In the present work, standardization of the kinetic parameters has been performed for achieving the purification and characterization of acid phosphatase which are currently underway.
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