A method for producing a recombinant collagen-like protein (CLP) can be performed. The method includes fermenting a host cell, accumulating the CLP in a medium to obtain a fermentation broth, separating the host cell from the fermentation broth to obtain a supernatant, and incubating the supernatant. The CLP can be purified after incubation.

Provided herein are methods, organisms, and tools for producing glycolic acid from ethylene glycol, and glycolic acid produced thereby.

The present invention provides polynucleotide vectors for high expression of heterologous genes. Some vectors further comprise novel transposons and transposases that further improve expression. Further disclosed are vectors that can be used in a gene transfer system for stably introducing nucleic acids into the DNA of a cell. The gene transfer systems can be used in methods, for example, gene expression, bioprocessing, gene therapy, insertional mutagenesis, or gene discovery.

This application describes consortium between fungi and algae, where the algae are incorporated within hyphae of the fungi. The fungi, the algae, or both can be modified to express heterologous lipid synthesizing enzymes. Incorporation of algae into fungi facilitates harvesting of the algae and products produced by the consortia. Such consortia are robust. For example, the fungi and algae can symbiotically provide nutrients to each other and are tolerant of environmental stresses.

Provided is a highly efficient ethanol-fermentative yeast having high efficiency in ethanol production without introducing a foreign gene. The highly efficient ethanol-fermentative yeast is a fermentative yeast that effectively produces ethanol from pentose and hexose and is deposited to NITE Patent Microorganisms Depositary under the accession number NITE BP-01962.

The present invention is directed to compositions comprising hydrolase-secreting bacteria and fermenting microorganisms and use thereof, such as for fermentative production of ethanol.

Pichia pastoris alcohol dehydrogenase 2 (ADH2) promoter variants include at least one of the specified modifications on wild-type Pichia pastoris ADH2 promoter (SEQ ID NO: 1). The modification includes one of the following mutations: integration of a Cat8 transcription factor binding site (TFBS), particularly integration of SEQ ID NO: 3 or other gene sequences that show at least 80% similarity with this sequence, at any positions within nucleotides a) 647 to 660; b) 739 to 752; c) 1 to 948; and d) mutations specified with SEQ ID NO: 2 within nucleotides 15 to 848 separately and combinations thereof.

The present invention provides polynucleotide vectors for high expression of heterologous genes. Some vectors further comprise novel transposons and transposases that further improve expression. Further disclosed are vectors that can be used in a gene transfer system for stably introducing nucleic acids into the DNA of a cell. The gene transfer systems can be used in methods, for example, gene expression, bioprocessing, gene therapy, insertional mutagenesis, or gene discovery.

A highly efficient ethanol-fermentative yeast having high efficiency in ethanol production is provided without introducing a foreign gene. The highly efficient ethanol-fermentative yeast features a fermentative yeast effectively producing ethanol from pentose and hexose and being deposited to NITE Patent Microorganisms Depositary under the accession number NITE BP-01963.

An object of the present invention is to obtain fermentative yeast having highly efficient ethanol production without introducing a foreign gene. A further object is to obtain a fermentative yeast that is resistant to proliferation inhibitors such as organic acids, which prevent the proliferation of the fermentative yeast. Meyerozyma guilliermondii that can produce ethanol effectively from pentose and hexose was isolated by breeding. Moreover, resistance was imparted to the fermentative yeast by introducing transaldolase and alcohol dehydrogenase genes derived from Meyerozyma guilliermondii into the fermentative yeast.