Heterologous expression and functional characterization of a plant alkaline phytase in Pichia pastoris (Record no. 53775)

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fixed length control field 02498nam a2200265Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
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control field 20250625162434.0
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Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-19652
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245 10 - TITLE STATEMENT
Title Heterologous expression and functional characterization of a plant alkaline phytase in Pichia pastoris
490 0# - SERIES STATEMENT
Volume/sequential designation Protein expression and purification, 74(2), p.196-203, 2010
520 3# - SUMMARY, ETC.
Summary, etc. Phytases catalyze the sequential hydrolysis of phytic acid (myo-insositol hexakisphosphate), the most abundant inositol phosphate in cells. Phytic acid constitutes 3-5 percent of the dry weight of cereal grains and legumes such as corn and soybean. The high concentration of phytates in animal feed and the inability of non-ruminant animals such as swine and poultry to digest phytates leads to phosphate contamination of soil and water bodies. The supplementation of animal feed with phytases results in increased bioavailability to animals and decreased environmental contamination. Therefore, phytases are of great commercial importance. Phytases with a range of properties are needed to address the specific digestive needs of different animals. Alkaline phytase (LlALP1 and LlALP2)which possess unique catalytic properties that have the potential to be useful as feed and food supplement has been identified in lily pollen. Substantial quantities of alkaline phytase are needed for animal feed studies. In this paper, we report the heterologous expression of LlALP2 from lily pollen in Pichia pastoris. The expression of recombinant LlALP2 (rLlALP2)was optimized by varying the cDNA coding for LlALP2, host strain and growth conditions. The catalytic properties of recombinant LlALP2 were investigated extensively (substrate specificity, pH- and temperature dependence, and the effect of Ca(2+), EDTA and inhibitors)and found to be very similar to that of the native LlALP2 indicating that rLlALP2 from P. pastoris can serve as a potential source for structural and animal feed studies.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element ALKALINE PHYTASE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PHOSPHATE CONTAMINATION
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element ANIMAL FEED
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element HETEROLOGOUS PROTEIN EXPRESSION
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PICHIA PASTORIS
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element POLLEN GRAINS
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Johnson, S. C.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Yang, M.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Murthy, P. P.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1hhfiEyHn8OPrINBNgmxErcxIeUaiDLWB/view?usp=drivesdk">https://drive.google.com/file/d/1hhfiEyHn8OPrINBNgmxErcxIeUaiDLWB/view?usp=drivesdk</a>
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Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-19652 25.06.2025 25.06.2025 Documentos solicitados