Patent classifications
C12N15/81
PRODUCTION OF MEVALONATE, ISOPRENE, AND ISOPRENOIDS USING GENES ENCODING POLYPEPTIDES HAVING THIOLASE, HMG-COA SYNTHASE AND HMG-COA REDUCTASE ENZYMATIC ACTIVITIES
The invention features compositions and methods for the increased production of mevalonate, isoprene, isoprenoid precursor molecules, and/or isoprenoids in microorganisms via the heterologous expression of the mvaE and mvaS genes from the organisms Listeria grayi DSM 20601, Enterococcus faecium, Enterococcus gallinarum EG2, and Enterococcus casseliflavus.
PROTEIN EXPRESSION STRAINS
The invention provides an improved host strain for production of desired protein.
A CRISPR-CAS SYSTEM FOR A YEAST HOST CELL
The present invention relates to the field of molecular biology and cell biology. More specifically, the present invention relates to a CRISPR-CAS system for a yeast host cell.
NUCLEIC ACID-GUIDED EDITING OF EXOGENOUS POLYNUCLEOTIDES IN HETEROLOGOUS CELLS
The present disclosure provides shuttle vectors for editing exogenous polynucleotides in heterologous live cells, as well as automated methods, modules, and multi-module cell editing instruments and systems for performing the editing methods.
NUCLEIC ACID-GUIDED EDITING OF EXOGENOUS POLYNUCLEOTIDES IN HETEROLOGOUS CELLS
The present disclosure provides shuttle vectors for editing exogenous polynucleotides in heterologous live cells, as well as automated methods, modules, and multi-module cell editing instruments and systems for performing the editing methods.
PROCESS FOR PRODUCING ETHANOL FROM RAW STARCH USING ALPHA-AMYLASE VARIANTS
The present invention relates to raw starch hydrolysis and in particular to a raw starch hydrolysis and fermentation process. More particularly the present invention relates to a process of producing a fermentation product from raw starch material, comprising the steps of: (a) saccharifying starch-containing material at a temperature below the initial gelatinization temperature of said starch-containing material; and (b) fermenting with a fermenting organism, wherein step (a) is carried out using at least a variant alpha-amylase comprising a substitution at one or more positions corresponding to positions 196, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 28, 38, 39, 43, 54, 56, 57, 64, 67, 68, 70, 71, 86, 89, 90, 94, 96, 99, 101, 103, 107, 108, 110, 113, 114, 117, 127, 134, 138, 142, 150, 151, 152, 156, 169, 171, 174, 179, 183, 193, 199, 200, 204, 205, 207, 208, 209, 212, 218, 221, 222, 224, 233, 241, 245, 259, 275, 278, 281, 282, 283, 284, 285, 308, 323, 335, 348, 359, 382, 386, 388, 392, 394, 396, 412, 414, 417, 424, 428, 457, 459, 466, 479, 489, 511, 533, 534, 542, 543, 545, 547, 549, 550, 551, 560, 566, 570, 574, 575, 576, 577, 578, 580, 581, 582, 589, 592, 599, 603, 605, 608, 614, 619, or 626 of the polypeptide of SEQ ID NO: 1, wherein the variant has alpha-amylase activity and wherein the variant has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity, but less than 100% sequence identity, to the polypeptide of SEQ ID NO: 1, and optionally a glucoamylase.
PROCESS FOR PRODUCING ETHANOL FROM RAW STARCH USING ALPHA-AMYLASE VARIANTS
The present invention relates to raw starch hydrolysis and in particular to a raw starch hydrolysis and fermentation process. More particularly the present invention relates to a process of producing a fermentation product from raw starch material, comprising the steps of: (a) saccharifying starch-containing material at a temperature below the initial gelatinization temperature of said starch-containing material; and (b) fermenting with a fermenting organism, wherein step (a) is carried out using at least a variant alpha-amylase comprising a substitution at one or more positions corresponding to positions 196, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 28, 38, 39, 43, 54, 56, 57, 64, 67, 68, 70, 71, 86, 89, 90, 94, 96, 99, 101, 103, 107, 108, 110, 113, 114, 117, 127, 134, 138, 142, 150, 151, 152, 156, 169, 171, 174, 179, 183, 193, 199, 200, 204, 205, 207, 208, 209, 212, 218, 221, 222, 224, 233, 241, 245, 259, 275, 278, 281, 282, 283, 284, 285, 308, 323, 335, 348, 359, 382, 386, 388, 392, 394, 396, 412, 414, 417, 424, 428, 457, 459, 466, 479, 489, 511, 533, 534, 542, 543, 545, 547, 549, 550, 551, 560, 566, 570, 574, 575, 576, 577, 578, 580, 581, 582, 589, 592, 599, 603, 605, 608, 614, 619, or 626 of the polypeptide of SEQ ID NO: 1, wherein the variant has alpha-amylase activity and wherein the variant has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% sequence identity, but less than 100% sequence identity, to the polypeptide of SEQ ID NO: 1, and optionally a glucoamylase.
REDUCTION IN ACETATE PRODUCTION BY YEAST OVER-EXPRESSING MIG3
Described are compositions and methods relating to modified yeast that over-express MIG transcriptional regulator polypeptides. The yeast produces a deceased amount of acetate compared to parental cells. Such yeast is particularly useful for large-scale ethanol production from starch substrates where acetate in an undesirable end product.
N-TERMINAL EXTENSION SEQUENCE FOR EXPRESSION OF RECOMBINANT THERAPEUTIC PEPTIDES
The invention relates to an N-terminal extension sequences which are employed to enhance the expression of recombinant therapeutic peptides. The invention also relates to a process for the high-level expression of recombinant therapeutic peptides using the said N-terminal extension sequence. The invention also provides nucleic acids, vectors and recombinant host cells for efficient production of biologically active proteins such as lirapeptide.
N-TERMINAL EXTENSION SEQUENCE FOR EXPRESSION OF RECOMBINANT THERAPEUTIC PEPTIDES
The invention relates to an N-terminal extension sequences which are employed to enhance the expression of recombinant therapeutic peptides. The invention also relates to a process for the high-level expression of recombinant therapeutic peptides using the said N-terminal extension sequence. The invention also provides nucleic acids, vectors and recombinant host cells for efficient production of biologically active proteins such as lirapeptide.