A series of independent human-induced non-transgenic mutations found at one or more of the SBEII genes of wheat; wheat plants having these mutations in one or more of their SBEII genes; and a method of creating and finding similar and/or additional mutations of SBEII by screening pooled and/or individual wheat plants. The seeds and flour from the wheat plants of the present invention exhibit an increase in amylose and resistant starch without having the inclusion of foreign nucleic acids in their genomes. Additionally, the wheat plants of the present invention exhibit altered SBEII activity without having the inclusion of foreign nucleic acids in their genomes.

A series of independent human-induced non-transgenic mutations found at one or more of the SBEII genes of wheat; wheat plants having these mutations in one or more of their SBEII genes; and a method of creating and finding similar and/or additional mutations of SBEII by screening pooled and/or individual wheat plants. The seeds and flour from the wheat plants of the present invention exhibit an increase in amylose and resistant starch without having the inclusion of foreign nucleic acids in their genomes. Additionally, the wheat plants of the present invention exhibit altered SBEII activity without having the inclusion of foreign nucleic acids in their genomes.

Provided are food and drink ingredients produced from wheat grain which has a low level (2-30%) of total starch branching enzyme II activity and an amylose content in the starch of at least 50% (w/w), and processes for producing and using the ingredients. Also provided are foods produced from the ingredients which may be used in humans to improve one or more parameters of metabolic health, bowel health or cardiovascular health.

The disclosure herein relates to a method for producing high-quality maltodextrin, and belongs to the technical field of maltodextrin. On the basis of a traditional enzymatic production process of maltodextrin, starch branching enzyme derived from Rhodothermus obamensis is introduced, an -1,4-glycosidic bond is cleaved, the cleaved short chain is ligated to a receptor chain to form an -1,6-branch point, so the degree of branching is increased and the maltodextrin has more cluster structures. Thereby, the aims that the stability of the maltodextrin is enhanced and the maltodextrin is not easy to retrograde are achieved, and the freeze-thaw stability of the maltodextrin is also improved. The method specifically comprises the steps of slurry preparation, spray liquefaction, starch branching enzyme action, filtration, decolorization, ion exchange, concentration, spray drying, and the like. The method can produce high-quality maltodextrin with good solubility and high transparency, good viscosity stability and good freeze-thaw stability during storage.

The present disclosure relates to acetaminophen protein adducts and methods of diagnosing acetaminophen toxicity using the acetaminophen protein adducts.

Disclosed is a method for modifying starch to slow down the digestion rate of modified starch. The present invention utilizes two-stage GBE treatment to convert the long straight-chain starch molecules into highly branched molecules with compact structures so as to decrease the digestion rate of the starch. During the two-stage treatment, granular starch was first treated with GBE, the treated starch was gelatinized in boiling water, and the gelatinized starch was treated with GBE for a second time, leading to an enhanced effect of GBE modification. Compared with the one-staged GBE modification, the two-stage GBE modification can further increase the content of slowly digestible starch in the modified starch and thus decrease the digestion rate of starch.

The present disclosure relates to acetaminophen protein adducts and methods of diagnosing acetaminophen toxicity using the acetaminophen protein adducts.

The present disclosure relates to acetaminophen protein adducts and methods of diagnosing acetaminophen toxicity using the acetaminophen protein adducts. The present disclosure provides acetaminophen (APAP)-protein adducts and methods of detecting acetaminophen-induced toxicity in a subject using APAP-protein adducts. One aspect of the present disclosure provides an APAP-protein adduct for diagnosing acetaminophen-induced toxicity. According to the present disclosure, the inventors have identified proteins that are modified by N-acetyl-pbenzoquinoneimine (NAPQI) in subjects with acetaminophen-induced toxicity. Non-limiting examples of proteins modified by NAPQI include betaine-homocysteine S-methyltransferase 1, cytoplasmic aspartate aminotransferase, 1,4-alpha-glucan branching enzyme, formimidoyltransferase-cyclodeaminase, and dystrophin.

The present disclosure relates to novel modular methods for generating a diversity of N-glycans of high mannose, hybrid and complex types. The present disclosure also relates to exemplary arrays of the synthesized N-glycans spotted onto aluminium oxide coated slides. These arrays can be used to detect and analyze binding interactions between the synthesized N-glycans and glycan binding molecules, such as HIV-1 neutralizing antibodies. The present disclosure also relates to methods for identifying agents that bind to various types of molecules on the arrays and to defining the structural elements of the molecules on the arrays that bind to those agents. The arrays and methods provided herein may be used for general epitope identification, drug discovery and as analytical tools. The present disclosure also provides useful glycans and epitope determinants that are useful in detecting, diagnosing, recurrence monitoring and preventing pathological diseases such as HIV.

Disclosed is a method for modifying starch to slow down the digestion rate of modified starch. The present invention utilizes two-stage GBE treatment to convert the long straight-chain starch molecules into highly branched molecules with compact structures so as to decrease the digestion rate of the starch. During the two-stage treatment, granular starch was first treated with GBE, the treated starch was gelatinized in boiling water, and the gelatinized starch was treated with GBE for a second time, leading to an enhanced effect of GBE modification. Compared with the one-staged GBE modification, the two-stage GBE modification can further increase the content of slowly digestible starch in the modified starch and thus decrease the digestion rate of starch.