Purification and Characterization, of Rice Bran Lipase II

Aizono, Yasuo; Funatsu, Masaru; Fujiki, Yukio; Watanabe, Masayoshi

doi:10.1080/00021369.1976.10862049

Cited by 21 publications

(27 citation statements)

References 3 publications

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“…Further, rice bran lipase I1 has different physico-chemical properties as compared to rice bran lipase I [3]. Later it has been shown that rice bran lipase contains subunits and differing in the molecular weight of the subunits.…”

Section: Introductionmentioning

confidence: 98%

“…Later it has been shown that rice bran lipase contains subunits and differing in the molecular weight of the subunits. Owing to presence of different lipases, AIZONO et al [3] have proposed the possibility of existence of multiple forms of rice bran lipase which means that rice bran lipase exists in differing their molecular weight, amino acid composition and the subunit structure.…”

Section: Introductionmentioning

confidence: 99%

“…In the case of rice, most of the lipase activities are present in the outer layers (bran) of the grains. The isolation and purification of rice bran lipase was carried out for the first time by FUNATSU et al [I] and SHASTRY et al [2] almost simultaneously and then Lipase I1 by AIZONO et al [3]. Subsequently, some of the chemical properties and the amino acid composition of the enzyme have been determined [4].…”

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of lipase from rice (Oryza sativa L.) bran

Rajeshwara¹,

Prakash²

1995

Nahrung

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SummaryLipase from defatted rice bran has been isolated by a new procedure which yields higher enzyme activity and quantity of enzyme. The procedure involves selective ammonium sulphate precipitation followed by ion exchange chromatography using DEAE-Sepharose CL-6B gel and column chromatography. The purified and homogeneous enzyme is also characterized for its various optical, enzymatic, physico-chemical and hydrodynamic properties. The enzyme has an ultraviolet absorption maximum at 276 nm with an extinction coefficient value of 15.25. The fluorescence excitation and cmission maximum values for the enzyme are 285 and 344 nm, respectively. The enzyme has a specific activity of 18 units [peq . mg-' . h-'1 with a pH optimum of 7.5 and a temperature optimum of 30 "C. The enzyme has an average hydrophobicity value of 3980 J/residue and the NPS (frequency of occurrance of non-polar side chains) and P (ratio of polar to non-polar amino acids) values are 0.29 and 1.13, respectively. The enzyme has a sedimentation coefficient value of 2.30 S and the isopotential partial specific volume is 0.697 ml/g. The molecular weight of the enzyme is 30000 and the enzyme is made up of at least two subunits. The enzyme contains 16% alpha-helix, 39% beta-structure and the rest being aperiodic. Zusammenfassung Reinigung und Charakterisierung von Lipase aus Reiskleie

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Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of lipase from rice (Oryza sativa L.) bran

Rajeshwara¹,

Prakash²

1995

Nahrung

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“…Three different kinds of lipases have been identified in rice bran. Two of them have thermal stability of 30 [30] and 408C [30] and the third one has thermal stability of over 1008C [31]. This would explain why lower levels of FFA are formed during storage for all types of rice flours dried at 1158C.…”

Section: Resultsmentioning

confidence: 96%

Method of creating starch‐like ultra‐fine rice flour and effect of spray drying on formation of free fatty acid

2010

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Rice flour from long, medium, and waxy grain cultivars were processed by passing a 32% rice flour slurry through a microfluidizer at 10 Â 10 4 kPa and spray dryer at three different outlet temperatures (50, 80, and 1158C). Spray-drying conditions were controlled by the flow rate of the slurry and inlet temperature. Spray-dried rice flours and unprocessed rice flour were examined for their lipolytic stability during storage for 210 days by measuring free fatty acid (FFA) formation. The percentage of lipid and FFA in rice flour was significantly reduced by spray drying. The resulting amount of lipid and percentage of FFA was rice-type dependent and related to the amylose content and the outlet temperature. Upon storage, the formation of FFA was lowest for rice flours processed at 1158C outlet temperature as compared to 808C, 508C, and control (untreated rice flour). Pin milling of the spray-dried flour resulted in the breakdown of loose re-agglomerated rice flour formed during spray drying with a particle size similar to rice starch but increased starch damage by about 1% per pass through pin mill.

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“…Los resultados de actividad específica de la lipasa para el extracto crudo y la fracción de sulfato amónico fueron similares a los publicados por Funatsu et al, (1971 ) y Aizono et al, (1976 (*) Media representativa de tres repeticiones. U = 1 jimol de nitrofenol liberado por minuto por mL de extracto la reacción.…”

Section: Rendimiento De Extracción Y Actividad Lipasaunclassified

Estudio comparativo de la obtención de extractos crudos y semipurificados de lipasa de salvado de arroz

Cruz¹,

Barrera‐Arellano²

1999

Grasas y Aceites

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RESUMENEstudio comparativo de la obtención de extractos crudos y semi-purifícados de lipasa de salvado de arroz.Los extractos crudos de lipasas de salvado de arroz desengrasado fueron obtenidos con tres diferentes soluciones de extracción: 1 -CaCb 0.01 M; 2 -Sacarosa 0.6M, KC110mM, MgCb 1 mM, Ditiotreitol 2mM; 3 -Sacarosa 0.4M, Ditiotreitol 2mM. Las variedades estudiadas pH (6.0, 7.0, 8.0) y tiempo de extracción (1h, 2h, 3h). La temperatura de extracción fue de 4 °C. Los extractos obtenidos presentaron diferentes actividades de lipasa siendo el extracto crudo obtenido con CaCl2 0.01 M el que mostró la mayor actividad específica (12. Imü/mg). La purificación parcial de este extracto crudo con acetona y sulfato amónico resultó en fracciones con actividad específica de 50.7mU/mg y 63.5mU/mg respectivamente. PALABRAS-CLAVE: Enzima -Extracción -Lipasa -Purificación -Salvado de arroz. SUMMARYComparative study of the obtention of crude and semi-purified lipase extracts from rice bran.Crude lipase extracts from defatted rice bran were obtained using three different extraction solutions: 1 -CaCb 0.01 M; 2 -Sacarose 0.6M, KCI lOmM, MgCb ImM, Ditiotreitol 2mM and 3 -Sacarose 0.4M, Ditiotreitol 2mM. Factors (variables) studied were pH (6.0, 7.0, 8.0) and extraction time (1h, 2h, 3h). Extraction temperature was 4 °C. The extracts obtained presented different lipase activities, and the crude extract obtained with CaCb 0.01 M was the one with the highest specific activity (12.1mU/mg). Partial purification of this crude extract with acetone and ammonium sulfate resulted in fractions with specific activities of 50.7mU/mg and 63.5mU/mg, respectively KEY-WORDS: Enzyme -Extraction -Lipase -PurificationRice bran.

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Purification and Characterization, of Rice Bran Lipase II

Cited by 21 publications

References 3 publications

Purification and characterization of lipase from rice (Oryza sativa L.) bran

Purification and characterization of lipase from rice (Oryza sativa L.) bran

Method of creating starch‐like ultra‐fine rice flour and effect of spray drying on formation of free fatty acid

Estudio comparativo de la obtención de extractos crudos y semipurificados de lipasa de salvado de arroz

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