A process of recovering oil, comprising (a) converting a starch-containing material into dextrins with an alpha-amylase; (b) saccharifying the dextrins using a carbohydrate source generating enzyme to form a sugar; (c) fermenting the sugar in a fermentation medium into a fermentation product using a fermenting organism; (d) recovering the fermentation product to form a whole stillage; (e) separating the whole stillage into thin stillage and wet cake; (e) optionally concentrating the thin stillage into syrup; (f) recovering oil from the thin stillage and/or optionally the syrup, wherein a protease and a phospholipase are present and/or added during steps (a) to (c). Use of a protease and a phospholipase for increasing oil recovery yields from thin stillage and/or syrup in a fermentation product production process.

The present invention relates to hybrid polypeptides having pullulanase activity, and polynucleotides encoding the polypeptides. The invention also relates to nucleic acid constructs, vectors, and host cells comprising the polynucleotides as well as methods of producing and using the polypeptides.

The present invention relates to pullulanase variants having increased thermoactivity and comprising substitutions of the parent pullulanase at one or more positions corresponding to positions 393, 143, 150, 243, 244, 345, 346, 368, 370, 373, 381, 382, 385, 387, 402, 429, 430, 431, 432, 456, 486, 492, 610, 624, 631, 632, 665 and 699 of the polypeptide of SEQ ID NO: 3. The present invention also relates to polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells comprising the polynucleotides; and methods of using the variants. The variants are mainly derived from pullulanases from Bacillus deramificans, Bacillus acidopullulyticus or hybrid pullulanases.

Methods of using thermostable serine proteases are described herein.

The present disclosure relates to a composition for improving muscle strength, containing, as an active ingredient, an Aureobasidium pullulans fermentation product produced by culturing Aureobasidium pullulans SM2001 (accession number KCCM 10307) in a medium containing rice bran enzyme lysate fermented using an amylase. According to the present disclosure, the amount of beta-glucan can be increased significantly as compared to a conventional Aureobasidium pullulans fermentation product and, thus, the effects on improvement of muscle strength and prevention or treatment of muscle diseases can be increased.

A Bacillus mojavensis H12 is disclosed, wherein the Bacillus mojavensis H12 was deposited in China General Microbiological Culture Collection Center on Apr. 23, 2023, with a deposit number of CGMCC No. 27186 and a classification name of Bacillus mojavensis, and a 16S rDNA sequence is shown in SEQ ID No. 1; a commercial high-molecular-weight pullulan is converted into a low-molecular-weight pullulan by utilizing the pullulanase producing property of Bacillus mojavensis H12, which provides a basis for the industrial production of the low-molecular-weight pullulan.

The present disclosure discloses a thermophilic recombinant type II pullulanase and the application thereof, and belongs to the technical field of genetic engineering. The present disclosure obtains a thermophilic recombinant type II pullulanase by heterologously expressing type II pullulanase in Escherichia coli. Its optimum pH is 6.6, it has better pH tolerance under the conditions of pH 5.8-8.0, and its optimum temperature is 95 C. After incubating at 95 C. for 10 h, the remaining enzyme activity is greater than 50%. It can exhibit higher specific enzyme activity under strong reducing conditions. For example, adding DTT to the culture environment can increase the specific enzyme activity of Sumo-Pul.sub.Py by 237.2%. The present disclosure also provides the combined truncation mutant 28N+791C of type II pullulanase Sumo-Pul.sub.Py. The specific enzyme activity of the enzyme mutant is 32.180.92 U/mg, which is 5.99 times as high as that of the wild-type enzyme, thereby having important industrial application value and potential.

The present invention relates to a variant pullulanase, having increased thermo-stability and/or increased thermo-activity compared to a parent pullulanase, comprising a substitution at least a one position selected from a position corresponding to positions 432, 486, 370, 17, 77, 103, 106, 107, 190, 196, 197, 262, 279, 283, 321, 367, 375, 382, 399, 401, 402, 411, 412, 434, 435, 443, 446, 459, 460, 479, 490, 498, 514, 529, 531, 533, 541, 545, 581, 583, 595, 649, 665, 688, 700, 709, 804, 811 of SEQ ID NO: 1, and optionally a deletion of one or more, e.g., all amino acids at positions 821, 822, 823, 824, 825, 826, 827, and 828, wherein the variant has pullulanase activity, and wherein the variant has 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%, but less than 100% sequence identity to a parent alpha amylase selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5. Further aspect the present invention relates to a process for liquefying starch-containing material at a temperature above the initial gelatinization temperature using an alpha-amylase and a thermo-stable pullulanase of the invention.

The invention provides liquid enzyme compositions which are physically and microbially stable. The compositions are used, for example, in beer brewing processes.

Described herein, inter cilia, are glucoamylase variants and methods of using the same for saccharifying a starch substrate. Moreover, the disclosure also relates to a process of producing fermentation products and a method for increasing starch digestibility in an animal as well as a method of producing a fermented beverage using said as well as a. method of producing a fermented beverage using said glucoamylase variants.